MolNFT v1 · #150151 · protein

Apo [fefe]-hydrogenase HYDA1 from chlamydomonas reinhardtii, variant C377H

6GL6 · Fe-hydrogenase: “Apo [fefe]-hydrogenase HYDA1 from chlamydomonas reinhardtii, variant C377H”. X-ray diffraction, 4 ligands (SF4, NA, CL), 4 pockets (best druggability 0.79). MolNFT v1 #150151 on GenesisL1: 3D structure, binding…

PDB: 6GL6
Type: protein
Length: 406 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fe-hydrogenase
EC: 1.18.99.1
UniProt: Q9FYU1
Ligands: SF4, NA, CL, SO3
Pockets: 4 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fe-hydrogenase (EC 1.18.99.1)	protein	406	44% helix, 16% strand	Q9FYU1

Ligands and binding sites

SF4 · Iron/sulfur cluster · ligand · chains A
NA · Sodium ion · metal · 2 copies · chains A
CL · Chloride ion · ion · chains A
SO3 · Sulfite ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 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	634	0.79	0.84	53	SF4, CL
2	50	0.55	0.90	17	empty
3	167	0.49	0.77	23	empty
4	56	0.28	0.74	20	empty

Compared structures

6GL6 · apo [FeFe]-hydrogenase HydA1 from Chlamydomonas reinhardtii, variant C377H · 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 Q9FYU1
Elsewhere: RCSB PDB 6GL6 · PDBe 6GL6 · UniProt Q9FYU1

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