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Nifs from hydrogenimonas thermopile in a persulfurated form

Analyse Nifs from hydrogenimonas thermopile in a persulfurated form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZST
Type: protein
Length: 773 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cysteine desulfurase
UniProt: A0A1I5NEH3
Pockets: 8 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cysteine desulfurase	protein	388	40% helix, 19% strand	A0A1I5NEH3
B	Cysteine desulfurase	protein	385	40% helix, 19% strand	A0A1I5NEH3

Pockets

8 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	150	0.82	0.98	25	empty
2	93	0.76	0.97	21	empty
3	428	0.63	0.77	42	empty
4	389	0.63	0.78	45	empty
5	113	0.36	0.73	18	empty

Interfaces

1 interface between chains.

A–B · 2619 Å² buried · 39 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (cofactor, oxidation).

Compared structures

5ZST · NifS from Hydrogenimonas thermopile in a persulfurated form · 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 A0A1I5NEH3
Elsewhere: RCSB PDB 5ZST · PDBe 5ZST · UniProt A0A1I5NEH3

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