MolNFT v1 · #40128 · protein
Crystal structure of HEC1 ch domain
2IGP · Retinoblastoma-associated protein hec: “Crystal structure of HEC1 ch domain”. X-ray diffraction. MolNFT v1 #40128 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2IGP
- Type
- protein
- Length
- 114 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinoblastoma-associated protein hec
- UniProt
- O14777
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinoblastoma-associated protein hec | protein | 114 | 54% helix, 0% strand | O14777 |
Ligands and binding sites
- BME · Beta-mercaptoethanol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 covalent (additive adduct).
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 O14777
- Elsewhere: RCSB PDB 2IGP · PDBe 2IGP · UniProt O14777
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