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Crystal structure of fox-4 cephamycinase complexed with sulfate

Analyse Crystal structure of fox-4 cephamycinase complexed with sulfate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CHU
Type: protein
Length: 718 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: Q9L387
Ligands: ZN, SO4
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Beta-lactamase (EC 3.5.2.6)	protein	359	40% helix, 23% strand	Q9L387

Ligands and binding sites

ZN · Zinc ion · metal · 8 copies · chains A, B
SO4 · Sulfate ion · ion · 4 copies · chains A, B
ACT · Acetate ion · additive · 2 copies · chains B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	824	0.74	0.79	89	SO4
2	275	0.57	0.77	36	empty
3	142	0.50	0.79	26	SO4
4	94	0.42	0.78	16	empty
5	89	0.42	0.78	17	empty

Interfaces

1 interface between chains.

A–B · 456 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

5CHU · CRYSTAL STRUCTURE OF Fox-4 cephamycinase complexed with sulfate · 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 Q9L387
Elsewhere: RCSB PDB 5CHU · PDBe 5CHU · UniProt Q9L387

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