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Crystal structure of the fourth and fifth fibronectin F1 modules in complex with a fragment of staphylococcus aureus fnbpa-5
Analyse Crystal structure of the fourth and fifth fibronectin F1 modules in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RL0
- Type
- protein
- Length
- 620 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibronectin; Fibronectin-binding protein
- UniProt
- P02751, P14738
- Pockets
- 9 · best druggability 0.78
Structure
x-ray diffraction · 7 distinct chains · 0% helix, 63% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, K | Fibronectin | protein | 89 | 0% helix, 61% strand | P02751 |
| G | Fibronectin-binding protein | protein | 17 | 0% helix, 71% strand | P14738 |
| C, H, L | Fibronectin-binding protein | protein | 17 | 0% helix, 71% strand | P14738 |
| E | Fibronectin-binding protein | protein | 16 | 0% helix, 63% strand | P14738 |
| F | Fibronectin | protein | 88 | 0% helix, 61% strand | P02751 |
| I | Fibronectin | protein | 79 | 0% helix, 59% strand | P02751 |
| J | Fibronectin-binding protein | protein | 13 | 0% helix, 85% strand | P14738 |
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1012 | 0.78 | 0.80 | 112 | empty |
| 2 | 947 | 0.77 | 0.80 | 115 | empty |
| 3 | 86 | 0.54 | 0.85 | 17 | empty |
| 4 | 60 | 0.53 | 0.88 | 18 | empty |
| 5 | 85 | 0.53 | 0.85 | 19 | empty |
Interfaces
24 interfaces between chains.
- A–G · 1109 Ų buried · 30 hydrogen bonds · protein-protein
- B–C · 1074 Ų buried · 32 hydrogen bonds · protein-protein
- D–E · 1065 Ų buried · 26 hydrogen bonds · protein-protein
- K–L · 1061 Ų buried · 29 hydrogen bonds · protein-protein
- F–H · 1002 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 disulfide (disulfide).
Compared structures
- 2RL0 · Crystal structure of the fourth and fifth fibronectin F1 modules in complex with a… · the same entry in another collection · chain L against L, 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 P02751
- Every structure of UniProt P14738
- Elsewhere: RCSB PDB 2RL0 · PDBe 2RL0 · UniProt P02751 · UniProt P14738
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