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Structural and catalytic characterization of molinate hydrolase
Analyse Structural and catalytic characterization of molinate hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UB9
- Type
- protein
- Length
- 3,736 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Molinate hydrolase
- UniProt
- G2XLB0
- Ligands
- ZN
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Molinate hydrolase | protein | 467 | 38% helix, 19% strand | G2XLB0 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
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 | 71 | 0.75 | 0.98 | 22 | ZN |
| 2 | 73 | 0.75 | 0.98 | 20 | ZN |
| 3 | 70 | 0.74 | 0.98 | 23 | ZN |
| 4 | 72 | 0.74 | 0.98 | 21 | ZN |
| 5 | 67 | 0.74 | 0.98 | 20 | ZN |
Interfaces
13 interfaces between chains.
- A–C · 1734 Ų buried · 48 hydrogen bonds · protein-protein
- B–D · 1719 Ų buried · 42 hydrogen bonds · protein-protein
- A–B · 1335 Ų buried · 23 hydrogen bonds · protein-protein
- C–D · 1330 Ų buried · 23 hydrogen bonds · protein-protein
- G–H · 1318 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 4UB9 · Structural and catalytic characterization of molinate hydrolase · the same entry in another collection · chain D against D, 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 G2XLB0
- Elsewhere: RCSB PDB 4UB9 · PDBe 4UB9 · UniProt G2XLB0
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