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Nifs from hydrogenimonas thermophila, soaked with L-cysteine for 8 min

Analyse Nifs from hydrogenimonas thermophila, soaked with L-cysteine for 8 min in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZSR
Type: protein
Length: 774 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cysteine desulfurase
UniProt: A0A1I5NEH3
Pockets: 7 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 41% 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	386	41% helix, 19% strand	A0A1I5NEH3

Pockets

7 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	155	0.82	0.97	25	empty
2	99	0.76	0.97	22	empty
3	384	0.63	0.78	48	empty
4	401	0.62	0.78	42	empty
5	121	0.37	0.73	18	empty

Interfaces

1 interface between chains.

A–B · 2588 Å² buried · 37 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (cofactor).

Compared structures

5ZSR · NifS from Hydrogenimonas thermophila, soaked with L-cysteine for 8 min · 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 5ZSR · PDBe 5ZSR · UniProt A0A1I5NEH3

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