Research workbench
Bamabcde bound to substrate espp in the intermediate-open espp state
Analyse Bamabcde bound to substrate espp in the intermediate-open espp state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TT6
- Type
- protein
- Length
- 915 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, W8SZY2, A0A1X3I1M6, A0A3L5AP29
- Pockets
- 16 · best druggability 0.82
Structure
electron microscopy · 5 distinct chains · 19% helix, 42% 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, 77% strand | Q7BSW5 |
| A | Outer membrane protein assembly factor bama | protein | 502 | 11% helix, 47% strand | C3TPJ2 |
| C | Outer membrane protein assembly factor bamc | protein | 34 | 12% helix, 0% strand | W8SZY2 |
| D | Outer membrane protein assembly factor bamd | protein | 141 | 73% helix, 0% strand | A0A1X3I1M6 |
| E | Outer membrane protein assembly factor bame | protein | 89 | 13% helix, 37% strand | A0A3L5AP29 |
Pockets
16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1112 | 0.82 | 0.83 | 114 | empty |
| 2 | 149 | 0.63 | 0.86 | 34 | empty |
| 3 | 324 | 0.62 | 0.79 | 38 | empty |
| 4 | 304 | 0.59 | 0.78 | 38 | empty |
| 5 | 270 | 0.55 | 0.77 | 33 | empty |
Interfaces
7 interfaces between chains.
- C–D · 1195 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 980 Ų buried · 14 hydrogen bonds · protein-protein
- A–E · 855 Ų buried · 13 hydrogen bonds · protein-protein
- D–E · 802 Ų buried · 13 hydrogen bonds · protein-protein
- P–A · 722 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 7TT6 · BamABCDE bound to substrate EspP in the intermediate-open EspP state · the same entry in another collection · chain P against P, TM-score 1.00
- Q7BSW5 · AlphaFold monomer V2.0 prediction for serine protease espp (Q7BSW5) · a predicted model of the same protein · chain P against A, TM-score 0.47
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 W8SZY2
- Every structure of UniProt A0A1X3I1M6
- Every structure of UniProt A0A3L5AP29
- Elsewhere: RCSB PDB 7TT6 · PDBe 7TT6 · UniProt Q7BSW5 · UniProt C3TPJ2 · UniProt W8SZY2 · UniProt A0A1X3I1M6 · UniProt A0A3L5AP29
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