MolNFT v1 · #75542 · protein

The refined crystallographic structure of a dd-peptidase penicillin- target enzyme at 1.6 a resolution

3PTE · D-alanyl-D-alanine carboxypeptidase transpeptidase: “The refined crystallographic structure of a dd-peptidase penicillin- target enzyme at 1.6 a resolution”. X-ray diffraction, 1 pocket (best druggability 0.56). MolNFT v1 #75542 on…

PDB: 3PTE
Type: protein
Length: 347 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-alanyl-D-alanine carboxypeptidase transpeptidase
EC: 3.4.16.4
UniProt: P15555
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D-alanyl-D-alanine carboxypeptidase transpeptidase (EC 3.4.16.4)	protein	347	35% helix, 19% strand	P15555

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	276	0.56	0.77	33	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3PTE · The refined crystallographic structure of a dd-peptidase penicillin-target enzyme at 1.6… · the same entry in another collection · chain A against A, TM-score 1.00
P15555 · AlphaFold monomer V2.0 prediction for D-alanyl-D-alanine carboxypeptidase (P15555) · a predicted model of the same protein · 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
Every structure of UniProt P15555
Elsewhere: RCSB PDB 3PTE · PDBe 3PTE · UniProt P15555

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