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Crystal structure of substrate-free form of pcya

Analyse Crystal structure of substrate-free form of pcya in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2DKE
Type: protein
Length: 241 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: CL
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PHYCOCYANOBILIN:FERREDOXIN oxidoreductase (EC 1.3.7.5)	protein	241	40% helix, 26% strand	Q55891

Ligands and binding sites

CL · Chloride ion · ion · chains A

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

Pockets

2 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	255	0.63	0.81	38	empty
2	53	0.31	0.76	17	empty

Compared structures

2DKE · Crystal structure of substrate-free form of 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 2DKE · PDBe 2DKE · UniProt Q55891

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