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Crystal structure of a AMINOPEPTIDASE/GLUCANASE homolog

Analyse Crystal structure of a AMINOPEPTIDASE/GLUCANASE homolog in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VHE
Type: protein
Length: 365 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AMINOPEPTIDASE/GLUCANASE homolog
UniProt: P94521
Ligands: ZN
Pockets: 2 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	AMINOPEPTIDASE/GLUCANASE homolog	protein	365	30% helix, 27% strand	P94521

Ligands and binding sites

ZN · Zinc ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	105	0.38	0.75	23	empty
2	54	0.31	0.77	14	empty

Modifications

Observed in the structure: 11 modified (engineered).

Compared structures

1VHE · Crystal structure of a aminopeptidase/glucanase homolog · the same entry in another collection · chain A against A, TM-score 1.00
P94521 · AlphaFold monomer V2.0 prediction for putative aminopeptidase ysdc (P94521) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P94521
Elsewhere: RCSB PDB 1VHE · PDBe 1VHE · UniProt P94521

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