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Crystal structure of formate dehydrogenase FDH2 enzyme from granulicella mallensis MP5ACTX8 in complex with NAD and azide.

Analyse Crystal structure of formate dehydrogenase FDH2 enzyme from granulicella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6T8J
Type: protein
Length: 1,494 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Formate dehydrogenase
EC: 1.17.1.9
UniProt: G8NTI5
Pockets: 15 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Formate dehydrogenase (EC 1.17.1.9)	protein	374	36% helix, 17% strand	G8NTI5
B, D	Formate dehydrogenase (EC 1.17.1.9)	protein	373	36% helix, 17% strand	G8NTI5

Pockets

15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1193	0.78	0.80	90	empty
2	1106	0.76	0.78	79	empty
3	794	0.74	0.78	87	empty
4	476	0.71	0.81	50	empty
5	60	0.60	0.91	15	empty

Interfaces

3 interfaces between chains.

B–C · 3863 Å² buried · 43 hydrogen bonds · protein-protein
A–B · 794 Å² buried · 4 hydrogen bonds · protein-protein
B–D · 175 Å² buried · 3 hydrogen bonds · protein-protein

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 G8NTI5
Elsewhere: RCSB PDB 6T8J · PDBe 6T8J · UniProt G8NTI5

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