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Structure of RPE65: P6522 crystal form grown in ammonium phosphate solution

Analyse Structure of RPE65: P6522 crystal form grown in ammonium phosphate solution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4F30
Type: protein
Length: 521 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Retinoid isomerohydrolase
EC: 3.1.1.64
UniProt: Q28175
Ligands: FE2, PO4
Pockets: 3 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Retinoid isomerohydrolase (EC 3.1.1.64)	protein	521	11% helix, 43% strand	Q28175

Ligands and binding sites

FE2 · Fe (II) ion · metal · chains A
PO4 · Phosphate ion · ion · 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	591	0.85	0.90	68	empty
2	516	0.79	0.86	53	empty
3	121	0.46	0.78	25	empty

Compared structures

4F30 · Structure of RPE65: P6522 crystal form grown in ammonium phosphate solution · the same entry in another collection · chain A against A, TM-score 1.00
Q28175 · AlphaFold monomer V2.0 prediction for retinoid isomerohydrolase (Q28175) · a predicted model of the same protein · 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 Q28175
Elsewhere: RCSB PDB 4F30 · PDBe 4F30 · UniProt Q28175

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