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The crystal structure of transhydrogenase from sinorhizobium meliloti

Analyse The crystal structure of transhydrogenase from sinorhizobium meliloti in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DIO
Type: protein
Length: 678 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD(P) transhydrogenase subunit alpha part 1
EC: 1.6.1.2
UniProt: F7X914
Pockets: 7 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NAD(P) transhydrogenase subunit alpha part 1 (EC 1.6.1.2)	protein	346	39% helix, 21% strand	F7X914
B	NAD(P) transhydrogenase subunit alpha part 1 (EC 1.6.1.2)	protein	332	39% helix, 21% strand	F7X914

Pockets

7 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	751	0.76	0.81	77	empty
2	451	0.74	0.84	44	empty
3	172	0.47	0.76	23	empty
4	160	0.45	0.75	25	empty
5	134	0.45	0.76	21	empty

Interfaces

1 interface between chains.

A–B · 1936 Å² buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 25 modified (engineered).

Compared structures

4DIO · The crystal structure of transhydrogenase from Sinorhizobium meliloti · 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 F7X914
Elsewhere: RCSB PDB 4DIO · PDBe 4DIO · UniProt F7X914

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