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Apo-form of dimeric 6-phosphogluconate dehydrogenase

Analyse Apo-form of dimeric 6-phosphogluconate dehydrogenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZYG
Type: protein
Length: 932 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 6-phosphogluconate dehydrogenase, decarboxylating
EC: 1.1.1.44
UniProt: Q762L5
Pockets: 4 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44)	protein	466	58% helix, 10% strand	Q762L5
B	6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44)	protein	466	58% helix, 10% strand	Q762L5

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1164	0.82	0.84	104	empty
2	745	0.68	0.75	56	empty
3	410	0.61	0.76	30	empty
4	277	0.53	0.75	43	empty

Interfaces

1 interface between chains.

A–B · 868 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

2ZYG · Apo-form of dimeric 6-phosphogluconate dehydrogenase · 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 Q762L5
Elsewhere: RCSB PDB 2ZYG · PDBe 2ZYG · UniProt Q762L5

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