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X-ray structure of the fefe-hydrogenase maturase hydg from carboxydothermus hydrogenoformans

Analyse X-ray structure of the fefe-hydrogenase maturase hydg from carboxydothermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RTB
Type: protein
Length: 429 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydg protein
UniProt: Q3ABV3
Ligands: SAM, SF4, CL
Pockets: 3 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydg protein	protein	429	51% helix, 11% strand	Q3ABV3

Ligands and binding sites

SAM · S-adenosylmethionine · ligand · chains A
SF4 · Iron/sulfur cluster · ligand · chains A
CL · Chloride ion · ion · 5 copies · chains A

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

Pockets

3 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	371	0.85	0.94	48	SAM, SF4
2	53	0.55	0.90	19	CL
3	69	0.35	0.77	17	empty

Compared structures

4RTB · X-ray structure of the FeFe-hydrogenase maturase HydG from Carboxydothermus… · 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 Q3ABV3
Elsewhere: RCSB PDB 4RTB · PDBe 4RTB · UniProt Q3ABV3

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