MolNFT v1 · #164817 · protein
Structure and molecular model refinement of aspergillus oryzae (taka) alpha-amylase: an application of the simulated-annealing method
6TAA: “Structure and molecular model refinement of aspergillus oryzae (taka) alpha-amylase: an application of the…”. X-ray diffraction, 1 ligand (CA). MolNFT v1 #164817 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6TAA
- Type
- protein
- Length
- 476 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P10529
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 476 | — | P10529 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6TAA · Structure and molecular model refinement of aspergillus oryzae (taka) alpha-amylase: an… · 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 P10529
- Elsewhere: RCSB PDB 6TAA · PDBe 6TAA · UniProt P10529
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.