Research workbench
Molybdate-activated form of mode from escherichia COLI
Analyse Molybdate-activated form of mode from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O7L
- Type
- protein
- Length
- 1,020 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator mode
- UniProt
- P46930
- Ligands
- CA, MOO, CL
- Pockets
- 14 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 30% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator mode | protein | 255 | 33% helix, 33% strand | P46930 |
| B | Transcriptional regulator mode | protein | 256 | 27% helix, 32% strand | P46930 |
| C | Transcriptional regulator mode | protein | 255 | 32% helix, 33% strand | P46930 |
| D | Transcriptional regulator mode | protein | 254 | 27% helix, 32% strand | P46930 |
Ligands and binding sites
- CA · Calcium ion · metal · chains B, C, D
- MOO · Molybdate ion · ion · 5 copies · chains A, B, C, D
- CL · Chloride ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 744 | 0.73 | 0.79 | 72 | empty |
| 2 | 446 | 0.68 | 0.80 | 78 | MOO, CA |
| 3 | 267 | 0.67 | 0.83 | 29 | empty |
| 4 | 105 | 0.63 | 0.88 | 19 | empty |
| 5 | 227 | 0.57 | 0.79 | 30 | empty |
Interfaces
5 interfaces between chains.
- A–B · 3447 Ų buried · 49 hydrogen bonds · protein-protein
- C–D · 3251 Ų buried · 42 hydrogen bonds · protein-protein
- B–D · 593 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 82 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 62 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1O7L · Molybdate-activated form of ModE from Escherichia coli · 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 P46930
- Elsewhere: RCSB PDB 1O7L · PDBe 1O7L · UniProt P46930
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