MolNFT v1 · #104146 · protein
Crystal structure of a putative dipeptidyl aminopeptidase IV (BACOVA_01349) from bacteroides ovatus atcc 8483 at 2.48 a resolution
4Q1V: “Crystal structure of a putative dipeptidyl aminopeptidase IV (BACOVA_01349) from bacteroides ovatus atcc 8483…”. X-ray diffraction, 1 ligand (MG), 13 pockets (best druggability 0.84). MolNFT v1 #104146 on GenesisL1: 3D structure…
- PDB
- 4Q1V
- Type
- protein
- Length
- 1,414 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative dipeptidyl aminopeptidase IV
- EC
- 3.4.-.-
- UniProt
- A7LU53
- Ligands
- MG
- Pockets
- 13 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative dipeptidyl aminopeptidase IV (EC 3.4.-.-) | protein | 707 | 18% helix, 38% strand | A7LU53 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 183 | 0.84 | 0.98 | 25 | empty |
| 2 | 247 | 0.68 | 0.85 | 35 | empty |
| 3 | 250 | 0.66 | 0.83 | 44 | empty |
| 4 | 236 | 0.61 | 0.81 | 43 | empty |
| 5 | 313 | 0.57 | 0.76 | 43 | empty |
Interfaces
1 interface between chains.
- A–B · 2132 Ų buried · 29 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 36 modified (engineered).
Compared structures
- 4Q1V · Crystal structure of a putative dipeptidyl aminopeptidase IV (BACOVA_01349) from… · 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 A7LU53
- Elsewhere: RCSB PDB 4Q1V · PDBe 4Q1V · UniProt A7LU53
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