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Crystal structure of bacterial peptidase

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

PDB: 7V6S
Type: protein
Length: 248 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Murein dd-endopeptidase MEPS/MUREIN ld-carboxypeptidase
EC: 3.4.17.13
UniProt: P0AFV4
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Murein dd-endopeptidase MEPS/MUREIN ld-carboxypeptidase (EC 3.4.17.13)	protein	124	29% helix, 30% strand	P0AFV4

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	255	0.51	0.75	40	empty

Interfaces

1 interface between chains.

A–B · 320 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

7V6S · Crystal structure of bacterial peptidase · the same entry in another collection · chain A against A, TM-score 1.00
P0AFV4 · AlphaFold monomer V2.0 prediction for murein dd-endopeptidase MEPS/MUREIN… · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P0AFV4
Elsewhere: RCSB PDB 7V6S · PDBe 7V6S · UniProt P0AFV4

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