MolNFT v1 · #90608 · protein

Crystal structure of H74E synechocystis sp. pcya sp. pcya

4EOD · PHYCOCYANOBILIN:FERREDOXIN oxidoreductase: “Crystal structure of H74E synechocystis sp. pcya sp. pcya”. X-ray diffraction, 2 ligands (BLA, CL), 3 pockets (best druggability 0.70). MolNFT v1 #90608 on GenesisL1: 3D structure, binding…

PDB: 4EOD
Type: protein
Length: 243 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: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PHYCOCYANOBILIN:FERREDOXIN oxidoreductase (EC 1.3.7.5)	protein	243	42% helix, 24% 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

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	245	0.70	0.85	38	BLA
2	52	0.31	0.76	18	empty
3	53	0.29	0.75	16	empty

Compared structures

4EOD · Crystal structure of H74E synechocystis sp. pcya 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 4EOD · PDBe 4EOD · UniProt Q55891

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