MolNFT v1 · #109389 · protein
Crystal structure of 4-ot from pseudomonas putida mt-2 with an enamine adduct on the N-terminal proline at 1.7 ångström resolution
4X1C · 2-hydroxymuconate tautomerase: “Crystal structure of 4-ot from pseudomonas putida mt-2 with an enamine adduct on the N-terminal proline at…”. X-ray diffraction, 1 ligand (NCO), 12 pockets (best druggability 0.82). MolNFT v1 #109389…
- PDB
- 4X1C
- Type
- protein
- Length
- 871 residues
- Chains
- 15
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2-hydroxymuconate tautomerase
- EC
- 5.3.2.6
- UniProt
- Q01468
- Ligands
- NCO
- Pockets
- 12 · best druggability 0.82
Structure
x-ray diffraction · 8 distinct chains · 44% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, N, O | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 58 | 43% helix, 33% strand | Q01468 |
| B | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 56 | 45% helix, 32% strand | Q01468 |
| C | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 58 | 43% helix, 33% strand | Q01468 |
| D, E | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 59 | 42% helix, 32% strand | Q01468 |
| F, I, J, M | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 57 | 44% helix, 33% strand | Q01468 |
| G | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 61 | 48% helix, 31% strand | Q01468 |
| H | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 62 | 47% helix, 31% strand | Q01468 |
| K, L | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 57 | 42% helix, 33% strand | Q01468 |
Ligands and binding sites
- NCO · Cobalt hexammine(iii) · ligand · 2 copies · chains B, C, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1008 | 0.82 | 0.84 | 102 | empty |
| 2 | 1159 | 0.79 | 0.81 | 104 | empty |
| 3 | 165 | 0.50 | 0.77 | 22 | empty |
| 4 | 186 | 0.49 | 0.76 | 25 | empty |
| 5 | 142 | 0.44 | 0.76 | 21 | empty |
Interfaces
39 interfaces between chains.
- G–J · 933 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 925 Ų buried · 7 hydrogen bonds · protein-protein
- I–L · 908 Ų buried · 10 hydrogen bonds · protein-protein
- E–F · 899 Ų buried · 8 hydrogen bonds · protein-protein
- H–K · 889 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (nonstandard).
Compared structures
- 4X1C · Crystal structure of 4-OT from Pseudomonas putida mt-2 with an enamine adduct on the… · the same entry in another collection · chain J against J, 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 Q01468
- Elsewhere: RCSB PDB 4X1C · PDBe 4X1C · UniProt Q01468
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