MolNFT v1 · #162905 · protein
Crystal structure of disulphide-linked human C3D dimer in complex with staphylococcus aureus complement subversion protein sbi-IV
6RMU: “Crystal structure of disulphide-linked human C3D dimer in complex with staphylococcus aureus complement…”. X-ray diffraction. MolNFT v1 #162905 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6RMU
- Type
- protein
- Length
- 727 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01024, Q931F4
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 299 | — | P01024 |
| C | — | protein | 62 | — | Q931F4 |
| B | — | protein | 300 | — | P01024 |
| D | — | protein | 66 | — | Q931F4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6RMU · Crystal structure of disulphide-linked human C3d dimer in complex with Staphylococcus… · the same entry in another collection · chain D against D, TM-score 1.00
- Q931F4 · AlphaFold monomer V2.0 prediction for immunoglobulin-binding protein sbi (Q931F4) · a predicted model of the same protein · chain C against A, TM-score 0.98
- P01024 · AlphaFold monomer V2.0 prediction for complement C3 (P01024) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 P01024
- Every structure of UniProt Q931F4
- Elsewhere: RCSB PDB 6RMU · PDBe 6RMU · UniProt P01024 · UniProt Q931F4
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