MolNFT v1 · #134304 · protein
Structural characterisation of mutant ASP39ALA of thioesterase (nmach) from neisseria meningitidis
5T02: “Structural characterisation of mutant ASP39ALA of thioesterase (nmach) from neisseria meningitidis”. X-ray diffraction, 3 ligands (GDP, COA, CL). MolNFT v1 #134304 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5T02
- Type
- protein
- Length
- 883 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0Y5D4F5
- Ligands
- GDP, COA, CL
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 146 | — | A0A0Y5D4F5 |
| B | — | protein | 147 | — | A0A0Y5D4F5 |
| C | — | protein | 150 | — | A0A0Y5D4F5 |
| D | — | protein | 148 | — | A0A0Y5D4F5 |
| E | — | protein | 147 | — | A0A0Y5D4F5 |
| F | — | protein | 145 | — | A0A0Y5D4F5 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F
- COA · Coenzyme A · ligand · 6 copies · chains A, B, C, D, E, F
- CL · Chloride ion · ion · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5T02 · Structural characterisation of mutant Asp39Ala of thioesterase (NmACH) from Neisseria… · 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 A0A0Y5D4F5
- Elsewhere: RCSB PDB 5T02 · PDBe 5T02 · UniProt A0A0Y5D4F5
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