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Putidaredoxin (FE2S2 ferredoxin), C73G mutant

Analyse Putidaredoxin (FE2S2 ferredoxin), C73G mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1R7S
Type: protein
Length: 318 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putidaredoxin
UniProt: P00259
Ligands: FES
Pockets: 3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Putidaredoxin	protein	106	22% helix, 22% strand	P00259

Ligands and binding sites

FES · Fe2/s2 (inorganic) cluster · ligand · 3 copies · chains A, B, C

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	253	0.55	0.77	30	empty
2	51	0.42	0.83	19	empty
3	82	0.41	0.79	16	empty

Interfaces

2 interfaces between chains.

B–C · 384 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 286 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

1R7S · PUTIDAREDOXIN (Fe2S2 ferredoxin), C73G mutant · the same entry in another collection · chain A against A, TM-score 1.00
P00259 · AlphaFold monomer V2.0 prediction for putidaredoxin (P00259) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P00259
Elsewhere: RCSB PDB 1R7S · PDBe 1R7S · UniProt P00259

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