Research workbench
CYP1 (HAP1) DNA-binding domain (residues 60-100), NMR, 15 structures
Analyse CYP1 (HAP1) DNA-binding domain (residues 60-100), NMR, 15 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PYC
- Type
- protein
- Length
- 41 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CYP1
- UniProt
- P12351
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 32% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CYP1 | protein | 41 | 32% helix, 5% strand | P12351 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1PYC · CYP1 (HAP1) DNA-binding domain (residues 60-100), NMR, 15 structures · 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 P12351
- Elsewhere: RCSB PDB 1PYC · PDBe 1PYC · UniProt P12351
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