MolNFT v1 · #10526 · protein

The X-ray crystal structure of pyrrolidone-carboxylate peptidase from hyperthermophilic archaeon pyrococcus horikoshii

1IU8: “The X-ray crystal structure of pyrrolidone-carboxylate peptidase from hyperthermophilic archaeon pyrococcus…”. X-ray diffraction, 1 pocket (best druggability 0.65). MolNFT v1 #10526 on GenesisL1: 3D structure, binding sites and…

PDB: 1IU8
Type: protein
Length: 412 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyrrolidone-carboxylate peptidase
EC: 3.4.19.3
UniProt: O58321
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pyrrolidone-carboxylate peptidase (EC 3.4.19.3)	protein	206	37% helix, 23% strand	O58321

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	509	0.65	0.76	61	empty

Interfaces

1 interface between chains.

A–B · 812 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

1IU8 · The X-ray Crystal Structure of Pyrrolidone-Carboxylate Peptidase from Hyperthermophilic… · the same entry in another collection · chain A against A, TM-score 1.00
O58321 · AlphaFold monomer V2.0 prediction for pyrrolidone-carboxylate peptidase (O58321) · 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 O58321
Elsewhere: RCSB PDB 1IU8 · PDBe 1IU8 · UniProt O58321

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