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[FeFe]-hydrogenase HydA1 from Chlamydomonas reinhardtii,variant E144A

Analyse [FeFe]-hydrogenase HydA1 from Chlamydomonas reinhardtii,variant E144A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GM7
Type: protein
Length: 410 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.14
Source: Chlamydomonas reinhardtii
Molecule: Fe-hydrogenase
EC: 1.18.99.1
UniProt: Q9FYU1
Ligands: SF4, CL
Pockets: 6 · best druggability 0.78

Structure

x-ray diffraction · resolution 2.14 · 1 distinct chain · 43% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fe-hydrogenase (EC 1.18.99.1)	protein	410	43% helix, 15% strand	Q9FYU1

Ligands and binding sites

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

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	672	0.78	0.83	54	SF4, CL
2	174	0.57	0.81	22	empty
3	72	0.53	0.86	23	empty
4	113	0.42	0.77	26	empty
5	54	0.33	0.77	16	empty

Compared structures

6GM7 · [fefe]-hydrogenase HYDA1 from chlamydomonas REINHARDTII,VARIANT E144A · 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 6GM7 · PDBe 6GM7 · UniProt Q9FYU1

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