Research workbench

Crystal structure of dipeptiase from pyrococcus horikoshii OT3

Analyse Crystal structure of dipeptiase from pyrococcus horikoshii OT3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WN1
Type: protein
Length: 712 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dipeptidase
EC: 3.4.-.-
UniProt: O58691
Ligands: CO
Pockets: 4 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dipeptidase (EC 3.4.-.-)	protein	356	36% helix, 25% strand	O58691

Ligands and binding sites

CO · Cobalt (II) ion · metal · 4 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	687	0.79	0.84	68	CO
2	443	0.70	0.81	42	CO
3	104	0.50	0.82	17	empty
4	123	0.47	0.79	16	empty

Interfaces

1 interface between chains.

A–B · 1270 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

1WN1 · Crystal Structure of Dipeptiase from Pyrococcus Horikoshii OT3 · the same entry in another collection · 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 O58691
Elsewhere: RCSB PDB 1WN1 · PDBe 1WN1 · UniProt O58691

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.