MolNFT v1 · #27704 · protein

Crystal structure of active site F1-mutant E213Q soaked with peptide phe-leu

1XRO · Proline iminopeptidase: “Crystal structure of active site F1-mutant E213Q soaked with peptide phe-leu”. X-ray diffraction, 1 ligand (LEU), 3 pockets (best druggability 0.73). MolNFT v1 #27704 on GenesisL1: 3D structure, binding…

PDB: 1XRO
Type: protein
Length: 290 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proline iminopeptidase
EC: 3.4.11.5
UniProt: P96084
Ligands: LEU
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proline iminopeptidase (EC 3.4.11.5)	protein	290	47% helix, 18% strand	P96084

Ligands and binding sites

LEU · Leucine · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.73	0.98	21	LEU
2	148	0.47	0.77	22	empty
3	64	0.30	0.74	15	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1XRO · Crystal structure of active site F1-mutant E213Q soaked with peptide Phe-Leu · the same entry in another collection · chain A against A, TM-score 1.00
P96084 · AlphaFold monomer V2.0 prediction for proline iminopeptidase (P96084) · 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 P96084
Elsewhere: RCSB PDB 1XRO · PDBe 1XRO · UniProt P96084

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