MolNFT v1 · #38298 · protein
Structure of the E. COLI GDP-mannose mannosyl hydrolase
2GT2: “Structure of the E. COLI GDP-mannose mannosyl hydrolase”. X-ray diffraction, 8 pockets (best druggability 0.79). MolNFT v1 #38298 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2GT2
- Type
- protein
- Length
- 608 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GDP-mannose mannosyl hydrolase
- EC
- 3.6.1.-
- UniProt
- P32056
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 30% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GDP-mannose mannosyl hydrolase (EC 3.6.1.-) | protein | 151 | 30% helix, 31% strand | P32056 |
| B | GDP-mannose mannosyl hydrolase (EC 3.6.1.-) | protein | 150 | 31% helix, 33% strand | P32056 |
| C | GDP-mannose mannosyl hydrolase (EC 3.6.1.-) | protein | 155 | 30% helix, 30% strand | P32056 |
| D | GDP-mannose mannosyl hydrolase (EC 3.6.1.-) | protein | 152 | 30% helix, 32% strand | P32056 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 897 | 0.79 | 0.81 | 80 | empty |
| 2 | 231 | 0.63 | 0.82 | 32 | empty |
| 3 | 239 | 0.60 | 0.80 | 32 | empty |
| 4 | 229 | 0.59 | 0.79 | 31 | empty |
| 5 | 221 | 0.56 | 0.79 | 35 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1414 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1397 Ų buried · 21 hydrogen bonds · protein-protein
- A–D · 434 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 257 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 200 Ų buried · 2 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 P32056
- Elsewhere: RCSB PDB 2GT2 · PDBe 2GT2 · UniProt P32056
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