Research workbench
PCSK9(DELTACRD) in complex with cyclic peptide 51
Analyse PCSK9(DELTACRD) in complex with cyclic peptide 51 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XID
- Type
- protein
- Length
- 390 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proprotein convertase SUBTILISIN/KEXIN type 9; Peptide 51
- EC
- 3.4.21.-
- UniProt
- Q8NBP7
- Ligands
- V7M
Structure
x-ray diffraction · 3 distinct chains · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proprotein convertase SUBTILISIN/KEXIN type 9 (EC 3.4.21.-) | protein | 92 | 30% helix, 39% strand | Q8NBP7 |
| B | Proprotein convertase SUBTILISIN/KEXIN type 9 (EC 3.4.21.-) | protein | 288 | 30% helix, 24% strand | Q8NBP7 |
| I | Peptide 51 | protein | 10 | 0% helix, 20% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
2 interfaces between chains.
- A–B · 1410 Ų buried · 29 hydrogen bonds · protein-protein
- B–I · 552 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide, 3 modified, 2 covalent, 1 d-amino (disulfide, nonstandard, covalent ligand, D-amino acid).
Compared structures
- 6XID · PCSK9(deltaCRD) in complex with cyclic peptide 51 · the same entry in another collection · chain A against A, 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 Q8NBP7
- Elsewhere: RCSB PDB 6XID · PDBe 6XID · UniProt Q8NBP7
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