MolNFT v1 · #9925 · protein
Crystal structure of inhibited interleukin-1BETA converting enzyme
1IBC: “Crystal structure of inhibited interleukin-1BETA converting enzyme”. X-ray diffraction, 1 ligand (ACE). MolNFT v1 #9925 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1IBC
- Type
- protein
- Length
- 259 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-1BETA converting enzyme; Peptide ACE-TRP-glu-his-asa
- EC
- 3.4.22.36
- UniProt
- P29466
- Ligands
- ACE
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-1BETA converting enzyme (EC 3.4.22.36) | protein | 167 | 34% helix, 21% strand | P29466 |
| B | Interleukin-1BETA converting enzyme (EC 3.4.22.36) | protein | 88 | 26% helix, 18% strand | P29466 |
| C | Peptide ACE-TRP-glu-his-asa | protein | 4 | 0% helix, 50% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 2651 Ų buried · 45 hydrogen bonds · protein-protein
- B–C · 444 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 236 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, nonstandard).
Compared structures
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 P29466
- Elsewhere: RCSB PDB 1IBC · PDBe 1IBC · UniProt P29466
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