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UniProt P04190

P04190

P04190 (UniProt P04190): 85 experimental structures and 1 predicted model on GenesisL1, 10 ligands bound. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
P04190
Experimental structures
85
Predicted models
1
Ligands
10

Structures

86 records of P04190 in the MolNFT archive: 85 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
1BC2Zn-dependent metallo-beta-lactamase from bacillus cereusx-ray diffractionA, B——
1BC2Zn-dependent metallo-beta-lactamase from bacillus cereusx-ray diffractionA, B——
1BMCStructure of a zinc metallo-beta-lactamase from bacillus cereusx-ray diffractionA——
1BMCStructure of a zinc metallo-beta-lactamase from bacillus cereusx-ray diffractionA——
1BVTMetallo-beta-lactamase from bacillus cereus 569/H/9x-ray diffractionA——
1BVTMetallo-beta-lactamase from bacillus cereus 569/H/9x-ray diffractionA——
1DXKMetallo-beta-lactamase from Bacillus cereus 569/H/9 C168S mutantx-ray diffractionA——
1DXKMetallo-beta-lactamase from bacillus cereus 569/H/9 C168S mutantx-ray diffractionA——
1MQOMetallo-beta-lactamase BcII Cd substituted from Bacillus cereus at 1.35 angstroms resolutionx-ray diffractionA——
1MQOMetallo-beta-lactamase bcii CD substituted from bacillus cereus at 1.35 ångströms resolutionx-ray diffractionA——
2BC2Metallo beta-lactamase II from bacillus cereus 569/H/9 at pH 6.0, trigonal crystal formx-ray diffractionA, B——
2BC2Metallo beta-lactamase II from bacillus cereus 569/H/9 at pH 6.0, trigonal crystal formx-ray diffractionA, B——
2BFKBacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH7 using 20mM ZnSO4…x-ray diffractionA, B——
2BFKBacillus cereus metallo-beta-lactamase (bcii) arg (121) cys mutant. solved at PH7 using 20MM ZNSO4…x-ray diffractionA, B——
2BFLBacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH5 using 20mM ZnSO4…x-ray diffractionA, B——
2BFLBacillus cereus metallo-beta-lactamase (bcii) arg (121) cys mutant. solved at PH5 using 20MM ZNSO4…x-ray diffractionA, B——
2BFZBacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH4.5 using 20mM…x-ray diffractionA, B——
2BFZBacillus cereus metallo-beta-lactamase (bcii) arg (121) cys mutant. solved at PH4.5 using 20MM…x-ray diffractionA, B——
2BG2Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH4.5 using 20mM…x-ray diffractionA, B——
2BG2Bacillus cereus metallo-beta-lactamase (bcii) arg (121) cys mutant. solved at PH4.5 using 20MM…x-ray diffractionA, B——
2BG6Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH5 using 20…x-ray diffractionA, B——
2BG6Bacillus cereus metallo-beta-lactamase (bcii) arg (121) cys mutant. solved at PH5 using 20…x-ray diffractionA, B——
2BG7Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH4.5 using 20…x-ray diffractionA, B——
2BG7Bacillus cereus metallo-beta-lactamase (bcii) arg (121) cys mutant. solved at PH4.5 using 20…x-ray diffractionA, B——
2BG8Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH4.5 using 20…x-ray diffractionA, B——
2BG8Bacillus cereus metallo-beta-lactamase (bcii) arg (121) cys mutant. solved at PH4.5 using 20…x-ray diffractionA, B——
2BGABacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH7 using 20…x-ray diffractionA, B——
2BGABacillus cereus metallo-beta-lactamase (bcii) arg (121) cys mutant. solved at PH7 using 20…x-ray diffractionA, B——
2M5CSolution Structure of the Bacillus cereus Metallo-Beta-Lactamase BcIIsolution nmrA——
2M5CSolution structure of the bacillus cereus metallo-beta-lactamase bciisolution nmrA——
2M5DSolution Structure of the Bacillus cereus Metallo-Beta-Lactamase BcII in Complex with…solution nmrA——
2M5DSolution structure of the bacillus cereus metallo-beta-lactamase bcii in complex with…solution nmrA——
2NXAStructure of Zn-dependent Metallo-Beta-Lactamase from Bacillus Cereus R121H, C221D Double Mutantx-ray diffractionA——
2NXAStructure of zn-dependent metallo-beta-lactamase from bacillus cereus R121H, C221D double mutantx-ray diffractionA——
2NYPStructure of beta-lactamase II from Bacillus cereus. R121H, C221D doble mutant with two zinc ions.x-ray diffractionA——
2NYPStructure of beta-lactamase II from bacillus cereus. R121H, C221D doble mutant with two zinc ions.x-ray diffractionA——
2NZEStructure of beta-lactamase II from Bacillus cereus. R121H, C221S double mutant. Space group P3121.x-ray diffractionA, B——
2NZEStructure of beta-lactamase II from bacillus cereus. R121H, C221S double mutant. space group P3121.x-ray diffractionA, B——
2NZFStructure of beta-lactamase II from Bacillus cereus. R121H, C221S double mutant. Space group C2.x-ray diffractionA——
2NZFStructure of beta-lactamase II from bacillus cereus. R121H, C221S double mutant. space group C2.x-ray diffractionA——
2UYXmetallo-beta-lactamase (1BC2) single point mutant D120Sx-ray diffractionA——
2UYXMetallo-beta-lactamase (1BC2) single point mutant D120Sx-ray diffractionA——
3BC2Metallo beta-lactamase II from bacillus cereus 569/H/9 at pH 6.0, monoclinic crystal formx-ray diffractionA——
3BC2Metallo beta-lactamase II from bacillus cereus 569/H/9 at pH 6.0, monoclinic crystal formx-ray diffractionA——
3FCZAdaptive protein evolution grants organismal fitness by improving catalysis and flexibilityx-ray diffractionA, B——
3FCZAdaptive protein evolution grants organismal fitness by improving catalysis and flexibilityx-ray diffractionA, B——
3I0VBacillus cereus metallo-beta-lactamase: apo formx-ray diffractionA——
3I0VBacillus cereus metallo-beta-lactamase: apo formx-ray diffractionA——
3I11Cobalt-substituted metallo-beta-lactamase from Bacillus cereusx-ray diffractionA——
3I11Cobalt-substituted metallo-beta-lactamase from bacillus cereusx-ray diffractionA——
3I13Bacillus cereus Zn-dependent metallo-beta-lactamase at pH 5.8x-ray diffractionA——
3I13Bacillus cereus zn-dependent metallo-beta-lactamase at pH 5.8x-ray diffractionA——
3I14Cobalt-substituted metallo-beta-lactamase from Bacillus cereus: residue Cys168 partially oxidizedx-ray diffractionA——
3I14Cobalt-substituted metallo-beta-lactamase from bacillus cereus: residue CYS168 partially oxidizedx-ray diffractionA——
3I15Cobalt-substituted metallo-beta-lactamase from Bacillus cereus: residue Cys168 fully oxidizedx-ray diffractionA——
3I15Cobalt-substituted metallo-beta-lactamase from bacillus cereus: residue CYS168 fully oxidizedx-ray diffractionA——
3KNRBacillus cereus metallo-beta-lactamase Cys221Asp mutant, 1 mM Zn(II)x-ray diffractionA, B, C, D——
3KNRBacillus cereus metallo-beta-lactamase CYS221ASP mutant, 1 mm ZN(II)x-ray diffractionA, B, C, D——
3KNSBacillus cereus metallo-beta-lactamase Cys221Asp mutant, 20 mM Zn(II)x-ray diffractionA, B, C, D——
3KNSBacillus cereus metallo-beta-lactamase CYS221ASP mutant, 20 mm ZN(II)x-ray diffractionA, B, C, D——

26 records more on the page itself.

Ligands

  • SO4 · Sulfate ion · in 8 records
  • ZN · Zinc ion · in 7 records
  • CF8 · (~{Z})-3-[2-(naphthalen-2-ylmethyl)phenyl]-2-sulfanyl-prop-2-enoic acid · in 2 records
  • BY5 · (~{Z})-2-sulfanyl-3-[2,3,6-tris(fluoranyl)phenyl]prop-2-enoic acid · in 1 record
  • C0W · (~{Z})-3-(1-benzothiophen-3-yl)-2-sulfanyl-prop-2-enoic acid · in 1 record
  • DZ5 · (2Z)-3-(4-fluorophenyl)-2-sulfanylprop-2-enoic acid · in 1 record
  • FE · Fe (III) ion · in 1 record
  • OH · Hydroxide ion · in 1 record
  • OK3 · (4~{R})-4-[[4-(aminomethyl)phenyl]carbonylamino]-3,3-bis(oxidanyl)-2-oxa-3-boranuidabicyclo[4.4.0]deca-1(10),6,8-triene-10-carboxylic acid · in 1 record
  • UNX · Unknown atom or ion · in 1 record

Experiment against prediction

Elsewhere

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