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DVAA-KlAte1

Analyse DVAA-KlAte1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7WG4
Type: protein
Length: 491 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.51
Source: Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /…
Molecule: Arginyltransferase
EC: 2.3.2.8
UniProt: Q6CXX6
Ligands: ZN
Pockets: 5 · best druggability 0.67

Structure

x-ray diffraction · resolution 1.51 · 1 distinct chain · 37% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Arginyltransferase (EC 2.3.2.8)	protein	491	37% helix, 22% strand	Q6CXX6

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

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	575	0.67	0.76	50	empty
2	255	0.61	0.80	36	empty
3	121	0.44	0.77	19	empty
4	77	0.43	0.80	19	empty
5	123	0.41	0.76	19	empty

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 Q6CXX6
Elsewhere: RCSB PDB 7WG4 · PDBe 7WG4 · UniProt Q6CXX6

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