Research workbench
Bamabcde bound to substrate espp in the open-sheet espp state
Analyse Bamabcde bound to substrate espp in the open-sheet espp state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TT5
- Type
- protein
- Length
- 928 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,SERINE protease espp chimera; Outer…
- EC
- 3.4.21.-
- UniProt
- Q7BSW5, C3TPJ2, A0A3L5AP29, A0A1X3I1M6, W8SZY2
- Pockets
- 15 · best druggability 0.82
Structure
electron microscopy · 5 distinct chains · 20% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,SERINE protease espp chimera (EC 3.4.21.-) | protein | 149 | 0% helix, 72% strand | Q7BSW5 |
| A | Outer membrane protein assembly factor bama | protein | 505 | 10% helix, 47% strand | C3TPJ2 |
| E | Outer membrane protein assembly factor bame | protein | 89 | 13% helix, 37% strand | A0A3L5AP29 |
| D | Outer membrane protein assembly factor bamd | protein | 153 | 78% helix, 0% strand | A0A1X3I1M6 |
| C | Outer membrane protein assembly factor bamc | protein | 32 | 9% helix, 0% strand | W8SZY2 |
Pockets
15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1120 | 0.82 | 0.83 | 117 | empty |
| 2 | 361 | 0.63 | 0.79 | 41 | empty |
| 3 | 130 | 0.62 | 0.86 | 31 | empty |
| 4 | 267 | 0.58 | 0.78 | 30 | empty |
| 5 | 273 | 0.57 | 0.78 | 35 | empty |
Interfaces
7 interfaces between chains.
- D–C · 1230 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 970 Ų buried · 14 hydrogen bonds · protein-protein
- A–E · 813 Ų buried · 9 hydrogen bonds · protein-protein
- E–D · 793 Ų buried · 8 hydrogen bonds · protein-protein
- P–A · 792 Ų buried · 24 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q7BSW5
- Every structure of UniProt C3TPJ2
- Every structure of UniProt A0A3L5AP29
- Every structure of UniProt A0A1X3I1M6
- Every structure of UniProt W8SZY2
- Elsewhere: RCSB PDB 7TT5 · PDBe 7TT5 · UniProt Q7BSW5 · UniProt C3TPJ2 · UniProt A0A3L5AP29 · UniProt A0A1X3I1M6 · UniProt W8SZY2
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