MolNFT v1 · #90720 · protein

Study on structure and function relationships in human pirin with cobalt ion

4ERO: “Study on structure and function relationships in human pirin with cobalt ion”. X-ray diffraction, 1 ligand (CO), 2 pockets (best druggability 0.65). MolNFT v1 #90720 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4ERO
Type: protein
Length: 288 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pirin
EC: 1.13.11.24
UniProt: O00625
Ligands: CO
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pirin (EC 1.13.11.24)	protein	288	8% helix, 49% strand	O00625

Ligands and binding sites

CO · Cobalt (II) ion · metal · chains A
EDO · 1,2-ethanediol · additive · 4 copies · 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	189	0.65	0.85	33	EDO
2	57	0.32	0.77	18	EDO

Compared structures

4ERO · Study on structure and function relationships in human Pirin with Cobalt ion · the same entry in another collection · chain A against A, TM-score 1.00
O00625 · AlphaFold monomer V2.0 prediction for pirin (O00625) · 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 O00625
Elsewhere: RCSB PDB 4ERO · PDBe 4ERO · UniProt O00625

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