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Crystal structure of H74Q synechocystis sp. pcya

Analyse Crystal structure of H74Q synechocystis sp. pcya in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EOC
Type: protein
Length: 239 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PHYCOCYANOBILIN:FERREDOXIN oxidoreductase
EC: 1.3.7.5
UniProt: Q55891
Ligands: BLA, CL
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PHYCOCYANOBILIN:FERREDOXIN oxidoreductase (EC 1.3.7.5)	protein	239	43% helix, 25% strand	Q55891

Ligands and binding sites

BLA · Biliverdine IX alpha · ligand · chains A
CL · Chloride ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	247	0.73	0.87	37	BLA

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

4EOC · Crystal structure of h74q Synechocystis sp. PCYA · the same entry in another collection · chain A against A, TM-score 1.00
Q55891 · AlphaFold monomer V2.0 prediction for PHYCOCYANOBILIN:FERREDOXIN oxidoreductase (Q55891) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q55891
Elsewhere: RCSB PDB 4EOC · PDBe 4EOC · UniProt Q55891

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