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X-ray structure of clavaminate synthase with vanadyl, succinate, and deoxyguanidinoproclavaminic acid

Analyse X-ray structure of clavaminate synthase with vanadyl, succinate, and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VWR
Type: protein
Length: 323 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Clavaminate synthase 3
EC: 1.14.11.21
UniProt: I0CBY7
Ligands: PCX, VVO
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Clavaminate synthase 3 (EC 1.14.11.21)	protein	323	30% helix, 22% strand	I0CBY7

Ligands and binding sites

PCX · Deoxyguanidinoproclavaminic acid · ligand · chains A
VVO · oxovanadium(2+) · ligand · chains A
SIN · Succinic 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	231	0.73	0.88	37	SIN, PCX, VVO

Compared structures

6VWR · X-ray structure of clavaminate synthase with vanadyl, succinate, and… · 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 I0CBY7
Elsewhere: RCSB PDB 6VWR · PDBe 6VWR · UniProt I0CBY7

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