MolNFT v1 · #118231 · protein

Crystal structure of beta-LACTAMASE/D-alanine carboxypeptidase from chromobacterium violaceum

5EVL: “Crystal structure of beta-LACTAMASE/D-alanine carboxypeptidase from chromobacterium violaceum”. X-ray diffraction, 2 ligands (SO4, CL), 2 pockets (best druggability 0.51). MolNFT v1 #118231 on GenesisL1: 3D structure, binding sites…

PDB: 5EVL
Type: protein
Length: 355 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: Q7NYG4
Ligands: SO4, CL
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	355	45% helix, 21% strand	Q7NYG4

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A
CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	137	0.51	0.80	27	SO4
2	54	0.27	0.74	15	SO4

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

5EVL · Crystal Structure of Beta-Lactamase/D-Alanine Carboxypeptidase from Chromobacterium… · 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
Every structure of UniProt Q7NYG4
Elsewhere: RCSB PDB 5EVL · PDBe 5EVL · UniProt Q7NYG4

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