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Crystal structure of a beta-lactamase-like protein from brucella melitensis bound to gmp

Analyse Crystal structure of a beta-lactamase-like protein from brucella melitensis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PY6
Type: protein
Length: 270 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase-like
UniProt: Q2YQ74
Ligands: 5GP, MN, K
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase-like	protein	270	24% helix, 31% strand	Q2YQ74

Ligands and binding sites

5GP · Guanosine-5'-monophosphate · ligand · chains A
MN · Manganese (II) ion · metal · 2 copies · chains A
K · Potassium ion · metal · chains A
TAR · D(-)-tartaric acid · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	54	0.29	0.75	10	empty

Compared structures

3PY6 · Crystal Structure of a Beta-Lactamase-Like Protein from Brucella Melitensis bound to GMP · 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 Q2YQ74
Elsewhere: RCSB PDB 3PY6 · PDBe 3PY6 · UniProt Q2YQ74

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