MolNFT v1 · #52392 · protein

Structure of the acyl-enzyme complex of an N-terminal nucleophile (ntn) hydrolase, OAT2

2VZK · Glutamate N-acetyltransferase 2 alpha chain: “Structure of the acyl-enzyme complex of an N-terminal nucleophile (ntn) hydrolase, OAT2”. X-ray diffraction, 14 pockets (best druggability 0.74). MolNFT v1 #52392 on GenesisL1: 3D…

PDB: 2VZK
Type: protein
Length: 1,507 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate N-acetyltransferase 2 alpha chain; Glutamate N-acetyltransferase 2 beta chain
EC: 2.3.1.35
UniProt: Q53940
Pockets: 14 · best druggability 0.74

Structure

x-ray diffraction · 5 distinct chains · 37% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, G	Glutamate N-acetyltransferase 2 alpha chain (EC 2.3.1.35)	protein	173	27% helix, 28% strand	Q53940
B	Glutamate N-acetyltransferase 2 beta chain (EC 2.3.1.35)	protein	213	40% helix, 25% strand	Q53940
D	Glutamate N-acetyltransferase 2 beta chain (EC 2.3.1.35)	protein	210	40% helix, 26% strand	Q53940
F	Glutamate N-acetyltransferase 2 beta chain (EC 2.3.1.35)	protein	197	39% helix, 27% strand	Q53940
H	Glutamate N-acetyltransferase 2 beta chain (EC 2.3.1.35)	protein	195	39% helix, 28% strand	Q53940

Ligands and binding sites

TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B
ACT · Acetate ion · additive · 2 copies · chains E, F, G, H

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1119	0.74	0.78	108	empty
2	921	0.72	0.77	89	empty
3	190	0.56	0.80	31	empty
4	201	0.53	0.78	33	empty
5	213	0.48	0.75	33	empty

Interfaces

18 interfaces between chains.

A–B · 2661 Å² buried · 59 hydrogen bonds · protein-protein
E–F · 2622 Å² buried · 58 hydrogen bonds · protein-protein
G–H · 2602 Å² buried · 58 hydrogen bonds · protein-protein
C–D · 2593 Å² buried · 60 hydrogen bonds · protein-protein
B–D · 363 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (nonstandard).

Compared structures

2VZK · Structure of the acyl-enzyme complex of an N-terminal nucleophile (Ntn) hydrolase, OAT2 · 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 Q53940
Elsewhere: RCSB PDB 2VZK · PDBe 2VZK · UniProt Q53940

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