MolNFT v1 · #174804 · protein

Structure of a mycobacterium tuberculosis puromycin-hydrolyzing peptidase

7C72 · Prolyl oligopeptidase: “Structure of a mycobacterium tuberculosis puromycin-hydrolyzing peptidase”. X-ray diffraction, 1 ligand (MLT), 13 pockets (best druggability 0.84). MolNFT v1 #174804 on GenesisL1: 3D structure, binding sites…

PDB: 7C72
Type: protein
Length: 1,302 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prolyl oligopeptidase
Ligands: MLT
Pockets: 13 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Prolyl oligopeptidase	protein	657	17% helix, 35% strand	—
B	Prolyl oligopeptidase	protein	645	17% helix, 34% strand	—

Ligands and binding sites

MLT · D-malate · ligand · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1190	0.84	0.85	100	empty
2	1197	0.80	0.82	97	empty
3	563	0.72	0.80	38	empty
4	582	0.72	0.80	39	empty
5	625	0.68	0.77	47	empty

Interfaces

1 interface between chains.

A–B · 927 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

7C72 · Structure of a mycobacterium tuberculosis puromycin-hydrolyzing peptidase · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 7C72 · PDBe 7C72

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