Research workbench
Crystal structure of human anti staphylococcus aureus antibody stau- 281 Fab in complex with isdb NEAT2 domain
Analyse Crystal structure of human anti staphylococcus aureus antibody stau- 281 Fab in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6P9H
- Type
- protein
- Length
- 1,079 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Iron-regulated heme-iron binding protein; Human anti staphylococcus aureus antibody…
- UniProt
- A0A1D4RDN9
- Pockets
- 10 · best druggability 0.67
Structure
x-ray diffraction · 6 distinct chains · 6% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Iron-regulated heme-iron binding protein | protein | 114 | 10% helix, 63% strand | A0A1D4RDN9 |
| C | Human anti staphylococcus aureus antibody stau-281 Fab heavy chain | protein | 213 | 4% helix, 49% strand | — |
| D | Human anti staphylococcus aureus antibody stau-281 Fab light chain | protein | 211 | 5% helix, 51% strand | — |
| A | Iron-regulated heme-iron binding protein | protein | 115 | 7% helix, 61% strand | A0A1D4RDN9 |
| H | Human anti staphylococcus aureus antibody stau-281 Fab heavy chain | protein | 214 | 6% helix, 51% strand | — |
| L | Human anti staphylococcus aureus antibody stau-281 Fab light chain | protein | 212 | 7% helix, 50% strand | — |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.67 | 0.91 | 22 | empty |
| 2 | 94 | 0.66 | 0.90 | 20 | empty |
| 3 | 387 | 0.56 | 0.74 | 49 | empty |
| 4 | 355 | 0.55 | 0.74 | 45 | empty |
| 5 | 114 | 0.39 | 0.75 | 21 | empty |
Interfaces
7 interfaces between chains.
- C–D · 1755 Ų buried · 13 hydrogen bonds · protein-protein
- H–L · 1716 Ų buried · 14 hydrogen bonds · protein-protein
- A–H · 894 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 857 Ų buried · 9 hydrogen bonds · protein-protein
- C–H · 516 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 6P9H · Crystal structure of human anti staphylococcus aureus antibody STAU-281 Fab in complex… · 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 A0A1D4RDN9
- Elsewhere: RCSB PDB 6P9H · PDBe 6P9H · UniProt A0A1D4RDN9
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