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Crystal structure of di-peptidase-E from xenopus laevis

Analyse Crystal structure of di-peptidase-E from xenopus laevis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7FFP
Type: protein
Length: 240 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-aspartyl dipeptidase
EC: 3.4.13.21
UniProt: Q91642
Ligands: ASP, CA
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-aspartyl dipeptidase (EC 3.4.13.21)	protein	240	29% helix, 23% strand	Q91642

Ligands and binding sites

ASP · Aspartic acid · ligand · chains A
CA · Calcium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.29	0.76	11	empty

Compared structures

7FFP · Crystal structure of di-peptidase-E from Xenopus laevis · the same entry in another collection · chain A against A, TM-score 1.00
Q91642 · AlphaFold monomer V2.0 prediction for alpha-aspartyl dipeptidase (Q91642) · 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 Q91642
Elsewhere: RCSB PDB 7FFP · PDBe 7FFP · UniProt Q91642

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