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Directed evolutionary changes in kemp eliminase KE07 - crystal 25 round 7

Analyse Directed evolutionary changes in kemp eliminase KE07 - crystal 25 round 7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6DC1
Type
protein
Length
3,020 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Ligands
6VP

Structure

x-ray diffraction · 8 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A, I, J—protein252——
B—protein252——
C, K—protein251——
D—protein250——
E, G—protein251——
F—protein256——
H—protein249——
L—protein253——

Ligands and binding sites

  • 6VP · 5-nitro-2-oxidanyl-benzenecarbonitrile · ligand · 4 copies · chains A, B, H, K
  • B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, D, B, C
  • PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains C, G
  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains L

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 6DC1 · Directed evolutionary changes in Kemp Eliminase KE07 - Crystal 25 round 7 · the same entry in another collection · chain A against A, TM-score 1.00

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