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Structure of transaminase ata-117 ARRMUT11 from arthrobacter sp. KNK168 inhibited with 1-(4-bromophenyl)-2-fluoroethylamine
Analyse Structure of transaminase ata-117 ARRMUT11 from arthrobacter sp. KNK168… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FR9
- Type
- protein
- Length
- 3,843 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- (R)-amine transaminase
- EC
- 2.6.1.18
- UniProt
- F7J696
- Ligands
- 9HC
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 5 distinct chains · 28% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, J, K | (R)-amine transaminase (EC 2.6.1.18) | protein | 319 | 28% helix, 26% strand | F7J696 |
| B, I | (R)-amine transaminase (EC 2.6.1.18) | protein | 320 | 28% helix, 27% strand | F7J696 |
| C, E, G, H | (R)-amine transaminase (EC 2.6.1.18) | protein | 321 | 27% helix, 26% strand | F7J696 |
| D, F | (R)-amine transaminase (EC 2.6.1.18) | protein | 322 | 27% helix, 26% strand | F7J696 |
| L | (R)-amine transaminase (EC 2.6.1.18) | protein | 318 | 28% helix, 27% strand | F7J696 |
Ligands and binding sites
- 9HC · [4-[3-(4-bromophenyl)-3-oxidanylidene-propyl]-6-methyl-5-oxidanyl-pyridin-3-yl]methyl phosphate · ligand · 12 copies · chains A, B, C, E, D, F, G, H, I, K, J, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 536 | 0.81 | 0.87 | 53 | 9HC |
| 2 | 553 | 0.80 | 0.86 | 55 | 9HC |
| 3 | 592 | 0.80 | 0.86 | 58 | 9HC |
| 4 | 558 | 0.80 | 0.86 | 55 | 9HC |
| 5 | 574 | 0.80 | 0.86 | 56 | 9HC |
Interfaces
22 interfaces between chains.
- D–F · 2205 Ų buried · 39 hydrogen bonds · protein-protein
- A–B · 2189 Ų buried · 38 hydrogen bonds · protein-protein
- G–H · 2174 Ų buried · 37 hydrogen bonds · protein-protein
- J–L · 2115 Ų buried · 35 hydrogen bonds · protein-protein
- C–E · 2035 Ų buried · 35 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 covalent, 6 disulfide (covalent ligand, disulfide).
Compared structures
- 5FR9 · Structure of transaminase ATA-117 arRmut11 from Arthrobacter sp. KNK168 inhibited with… · 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 F7J696
- Elsewhere: RCSB PDB 5FR9 · PDBe 5FR9 · UniProt F7J696
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