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Crystal structure of the hydrogenase assembly chaperone HYPC/HUPF family protein from shewanella oneidensis mr-1

Analyse Crystal structure of the hydrogenase assembly chaperone HYPC/HUPF family… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3D3R
Type: protein
Length: 163 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydrogenase assembly chaperone HYPC/HUPF
UniProt: Q8EF93
Pockets: 2 · best druggability 0.39

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydrogenase assembly chaperone HYPC/HUPF	protein	83	22% helix, 46% strand	Q8EF93
B	Hydrogenase assembly chaperone HYPC/HUPF	protein	80	31% helix, 41% strand	Q8EF93

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	88	0.39	0.77	16	empty
2	77	0.39	0.77	13	empty

Interfaces

1 interface between chains.

A–B · 2032 Å² buried · 28 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

3D3R · Crystal structure of the hydrogenase assembly chaperone HypC/HupF family protein from… · 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 Q8EF93
Elsewhere: RCSB PDB 3D3R · PDBe 3D3R · UniProt Q8EF93

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