Research workbench
Crystal structure of acpa E4 in complex with CEP1
Analyse Crystal structure of acpa E4 in complex with CEP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OCK
- Type
- protein
- Length
- 450 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Ligands
- CIR, ACA
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | — | protein | 215 | — | — |
| H | — | protein | 220 | — | — |
| A | — | protein | 15 | — | — |
Ligands and binding sites
- CIR · Citrulline · ligand · 2 copies · chains A, L, H
- ACA · 6-aminohexanoic acid · ligand · chains L, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OCK · Crystal structure of ACPA E4 in complex with CEP1 · the same entry in another collection · chain H against H, 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
- Elsewhere: RCSB PDB 5OCK · PDBe 5OCK
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