MolNFT v1 · #104201 · protein
Human D-dt complexed with tartrate
4Q3F · D-dopachrome decarboxylase: “Human D-dt complexed with tartrate”. X-ray diffraction, 3 pockets (best druggability 0.71). MolNFT v1 #104201 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4Q3F
- Type
- protein
- Length
- 351 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-dopachrome decarboxylase
- EC
- 4.1.1.84
- UniProt
- P30046
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | D-dopachrome decarboxylase (EC 4.1.1.84) | protein | 117 | 40% helix, 28% strand | P30046 |
Ligands and binding sites
- TLA · L(+)-tartaric acid · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1091 | 0.71 | 0.75 | 87 | TLA |
| 2 | 86 | 0.36 | 0.75 | 16 | TLA |
| 3 | 53 | 0.32 | 0.77 | 13 | TLA |
Interfaces
3 interfaces between chains.
- B–C · 286 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 176 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 91 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
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 P30046
- Elsewhere: RCSB PDB 4Q3F · PDBe 4Q3F · UniProt P30046
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