Research workbench
Asymmetric complex of factor XII and kininogen with GC1QR/C1QBP/P32 is governed by allostery
Analyse Asymmetric complex of factor XII and kininogen with GC1QR/C1QBP/P32 is governed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SZW
- Type
- protein
- Length
- 588 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement component 1 Q subcomponent-binding protein, mitochondrial; Coagulation factor…
- EC
- 3.4.21.38
- UniProt
- Q07021, P00748
- Ligands
- ZN
- Pockets
- 10 · best druggability 0.52
Structure
x-ray diffraction · 4 distinct chains · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement component 1 Q subcomponent-binding protein, mitochondrial | protein | 176 | 38% helix, 27% strand | Q07021 |
| B | Complement component 1 Q subcomponent-binding protein, mitochondrial | protein | 174 | 37% helix, 27% strand | Q07021 |
| C | Complement component 1 Q subcomponent-binding protein, mitochondrial | protein | 186 | 35% helix, 27% strand | Q07021 |
| D | Coagulation factor XII (EC 3.4.21.38) | protein | 52 | 13% helix, 31% strand | P00748 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.52 | 0.77 | 23 | empty |
| 2 | 163 | 0.49 | 0.77 | 21 | empty |
| 3 | 174 | 0.46 | 0.75 | 22 | empty |
| 4 | 145 | 0.45 | 0.76 | 25 | empty |
| 5 | 93 | 0.40 | 0.77 | 19 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1257 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 1240 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 1226 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 557 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6SZW · Asymmetric complex of Factor XII and kininogen with gC1qR/C1QBP/P32 is governed by… · the same entry in another collection · chain D against D, TM-score 1.00
- Q07021 · AlphaFold monomer V2.0 prediction for complement component 1 Q subcomponent-binding… · a predicted model of the same protein · chain B against A, TM-score 0.97
- P00748 · AlphaFold monomer V2.0 prediction for coagulation factor XII (P00748) · a predicted model of the same protein · chain D against A, TM-score 0.90
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 Q07021
- Every structure of UniProt P00748
- Elsewhere: RCSB PDB 6SZW · PDBe 6SZW · UniProt Q07021 · UniProt P00748
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