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Crystal structure of human thimet oligopeptidase.

Analyse Crystal structure of human thimet oligopeptidase. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1S4B
Type: protein
Length: 654 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thimet oligopeptidase
EC: 3.4.24.15
UniProt: P52888
Ligands: ZN
Pockets: 6 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
P	Thimet oligopeptidase (EC 3.4.24.15)	protein	654	60% helix, 8% strand	P52888

Ligands and binding sites

ZN · Zinc ion · metal · chains P

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

Pockets

6 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	943	0.76	0.78	86	empty
2	1083	0.73	0.76	81	empty
3	79	0.45	0.81	15	empty
4	53	0.35	0.79	17	empty
5	56	0.31	0.76	11	empty

Compared structures

1S4B · Crystal structure of human thimet oligopeptidase. · the same entry in another collection · chain P against P, TM-score 1.00
P52888 · AlphaFold monomer V2.0 prediction for thimet oligopeptidase (P52888) · a predicted model of the same protein · chain P against A, TM-score 0.88

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 P52888
Elsewhere: RCSB PDB 1S4B · PDBe 1S4B · UniProt P52888

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