MolNFT v2 · #197057 · protein
Cryogenic electron microscopy 3D map of F-actin bound by human dimeric alpha-catenin
7UTJ: “Cryogenic electron microscopy 3D map of F-actin bound by human dimeric alpha-catenin”. Electron microscopy at 2.77, 2 ligands (ADP, MG). MolNFT v2 #197057 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7UTJ
- Type
- protein
- Length
- 3,156 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.77
- Source
- Homo sapiens; Oryctolagus cuniculus
- UniProt
- P68135, P35221
- Ligands
- ADP, MG
Structure
electron microscopy · resolution 2.77 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 370 | — | P68135 |
| G, H, I, K, L, Z | — | protein | 156 | — | P35221 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F
- MG · Magnesium ion · metal · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain E against A, TM-score 0.96
- P35221 · AlphaFold monomer V2.0 prediction for catenin alpha-1 (P35221) · a predicted model of the same protein · chain H against A, TM-score 0.76
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 P68135
- Every structure of UniProt P35221
- Elsewhere: RCSB PDB 7UTJ · PDBe 7UTJ · UniProt P68135 · UniProt P35221
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