MolNFT v1 · #51337 · protein
Structure of a novel N-acyl-enzyme intermediate of an N- terminal nucleophile (ntn) hydrolase, OAT2
2V4I · Glutamate N-acetyltransferase 2 alpha chain: “Structure of a novel N-acyl-enzyme intermediate of an N- terminal nucleophile (ntn) hydrolase, OAT2”. X-ray diffraction, 13 pockets (best druggability 0.72). MolNFT v1 #51337 on…
- PDB
- 2V4I
- Type
- protein
- Length
- 1,504 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
- 13 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 26% 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, D, F, H | Glutamate N-acetyltransferase 2 beta chain (EC 2.3.1.35) | protein | 203 | 43% helix, 24% strand | Q53940 |
Pockets
13 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 296 | 0.72 | 0.85 | 42 | empty |
| 2 | 517 | 0.72 | 0.81 | 51 | empty |
| 3 | 645 | 0.69 | 0.78 | 59 | empty |
| 4 | 273 | 0.65 | 0.82 | 31 | empty |
| 5 | 240 | 0.64 | 0.82 | 32 | empty |
Interfaces
19 interfaces between chains.
- A–B · 2536 Ų buried · 54 hydrogen bonds · protein-protein
- G–H · 2520 Ų buried · 56 hydrogen bonds · protein-protein
- E–F · 2492 Ų buried · 52 hydrogen bonds · protein-protein
- C–D · 2488 Ų buried · 54 hydrogen bonds · protein-protein
- F–H · 1040 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (nonstandard).
Compared structures
- 2V4I · Structure of a novel N-acyl-enzyme intermediate of an N-terminal nucleophile (Ntn)… · the same entry in another collection · chain H against H, 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 2V4I · PDBe 2V4I · UniProt Q53940
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