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[fefe]-hydrogenase HYDA1 from chlamydomonas REINHARDTII,VARIANT E141Q

Analyse [fefe]-hydrogenase HYDA1 from chlamydomonas REINHARDTII,VARIANT E141Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GM6
Type: protein
Length: 409 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
Pockets: 5 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fe-hydrogenase (EC 1.18.99.1)	protein	409	44% helix, 15% strand	Q9FYU1

Ligands and binding sites

SF4 · Iron/sulfur cluster · ligand · chains A
NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · chains A

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

Pockets

5 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	653	0.79	0.84	60	SF4, CL
2	53	0.51	0.87	17	empty
3	156	0.48	0.77	22	empty
4	125	0.47	0.79	28	empty
5	52	0.28	0.75	19	empty

Compared structures

6GM6 · [FeFe]-hydrogenase HydA1 from Chlamydomonas reinhardtii,variant E141Q · 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 6GM6 · PDBe 6GM6 · UniProt Q9FYU1

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