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Crystal structure of pbpa from mycobacterium tuberculosis

Analyse Crystal structure of pbpa from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3LO7
Type
protein
Length
803 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Penicillin-binding protein a
EC
3.4.16.4
UniProt
P71586
Pockets
9 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APenicillin-binding protein a (EC 3.4.16.4)protein42034% helix, 21% strandP71586
BPenicillin-binding protein a (EC 3.4.16.4)protein38336% helix, 19% strandP71586

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1540.650.9520empty
21230.600.8625empty
32580.570.7836empty
42720.530.7639empty
51570.480.7733empty

Interfaces

1 interface between chains.

  • A–B · 833 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 3LO7 · Crystal structure of PBPA from Mycobacterium tuberculosis · the same entry in another collection · chain A against A, TM-score 1.00

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