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Crystal structure of glutathione-binding protein a (gbpa) from haemophilus parasuis SH0165 in complex with glutathione disulfide (gssg)

Analyse Crystal structure of glutathione-binding protein a (gbpa) from haemophilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3M8U
Type: protein
Length: 508 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heme-binding protein a
UniProt: B8F653
Ligands: GDS
Pockets: 4 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heme-binding protein a	protein	508	32% helix, 23% strand	B8F653

Ligands and binding sites

GDS · Oxidized glutathione disulfide · ligand · chains A
MLI · Malonate ion · additive · 3 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	741	0.82	0.86	94	GDS, MLI
2	131	0.72	0.92	31	empty
3	61	0.60	0.91	18	empty
4	109	0.35	0.73	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3M8U · Crystal structure of glutathione-binding protein A (GbpA) from Haemophilus parasuis… · 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 B8F653
Elsewhere: RCSB PDB 3M8U · PDBe 3M8U · UniProt B8F653

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