Research workbench
Structure of the EGF-like module of human C1R, NMR, 19 structures
Analyse Structure of the EGF-like module of human C1R, NMR, 19 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1APQ
- Type
- protein
- Length
- 53 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement protease C1R
- EC
- 3.4.21.41
- UniProt
- P00736
Structure
solution nmr · 1 distinct chain · 0% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement protease C1R (EC 3.4.21.41) | protein | 53 | 0% helix, 26% strand | P00736 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1APQ · Structure of the EGF-like module of human C1R, NMR, 19 structures · the same entry in another collection · chain A against A, TM-score 1.00
- P00736 · AlphaFold monomer V2.0 prediction for complement C1R subcomponent (P00736) · a predicted model of the same protein · chain A against A, TM-score 0.68
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 P00736
- Elsewhere: RCSB PDB 1APQ · PDBe 1APQ · UniProt P00736
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