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

Analyse Study on structure and function relationships in human pirin with manganese ion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EWE
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: MN
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pirin (EC 1.13.11.24)	protein	288	7% helix, 50% strand	O00625

Ligands and binding sites

MN · Manganese (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	199	0.67	0.86	35	EDO
2	51	0.29	0.76	18	EDO

Compared structures

4EWE · Study on structure and function relationships in human Pirin with Manganese 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 4EWE · PDBe 4EWE · UniProt O00625

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