Research workbench
Structure of the ustilago maydis chorismate mutase 1 in complex with KWL1-B from zea mays
Analyse Structure of the ustilago maydis chorismate mutase 1 in complex with KWL1-B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TI2
- Type
- protein
- Length
- 850 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chromosome 16, whole genome shotgun sequence; Ripening-related protein 3
- EC
- 5.4.99.5
- UniProt
- A0A0D1DWQ2, K7U7F7
- Pockets
- 13 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, C | Chromosome 16, whole genome shotgun sequence (EC 5.4.99.5) | protein | 262 | 61% helix, 2% strand | A0A0D1DWQ2 |
| E, A | Ripening-related protein 3 | protein | 163 | 4% helix, 30% strand | K7U7F7 |
Pockets
13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 742 | 0.78 | 0.82 | 71 | empty |
| 2 | 760 | 0.78 | 0.82 | 61 | empty |
| 3 | 193 | 0.77 | 0.92 | 28 | empty |
| 4 | 161 | 0.74 | 0.92 | 30 | empty |
| 5 | 86 | 0.71 | 0.94 | 20 | empty |
Interfaces
5 interfaces between chains.
- B–C · 2110 Ų buried · 33 hydrogen bonds · protein-protein
- C–A · 1306 Ų buried · 22 hydrogen bonds · protein-protein
- B–E · 1302 Ų buried · 26 hydrogen bonds · protein-protein
- B–A · 124 Ų buried · 2 hydrogen bonds · protein-protein
- C–E · 115 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 6TI2 · Structure of the Ustilago maydis chorismate mutase 1 in complex with KWL1-b from Zea mays · the same entry in another collection · chain B against B, 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 A0A0D1DWQ2
- Every structure of UniProt K7U7F7
- Elsewhere: RCSB PDB 6TI2 · PDBe 6TI2 · UniProt A0A0D1DWQ2 · UniProt K7U7F7
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