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Crystal structure of O-succinylbenzoate synthase from bdellovibrio bacteriovorus liganded with mg

Analyse Crystal structure of O-succinylbenzoate synthase from bdellovibrio… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CAW
Type: protein
Length: 632 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: O-succinylbenzoate synthase
UniProt: Q6MQC7
Ligands: MG
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	O-succinylbenzoate synthase	protein	316	37% helix, 21% strand	Q6MQC7

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

2 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	1101	0.80	0.82	104	empty
2	421	0.69	0.81	49	empty

Interfaces

1 interface between chains.

A–B · 707 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3CAW · Crystal structure of o-succinylbenzoate synthase from Bdellovibrio bacteriovorus liganded… · 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 Q6MQC7
Elsewhere: RCSB PDB 3CAW · PDBe 3CAW · UniProt Q6MQC7

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