MolNFT v1 · #15180 · protein
Crystal structure analysis of the hyperthermostable pyrocoocus woesei alpha-amylase
1MWO · Alpha amylase: “Crystal structure analysis of the hyperthermostable pyrocoocus woesei alpha-amylase”. X-ray diffraction, 2 ligands (ZN, CA), 2 pockets (best druggability 0.44). MolNFT v1 #15180 on GenesisL1: 3D structure, binding…
- PDB
- 1MWO
- Type
- protein
- Length
- 434 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha amylase
- EC
- 3.2.1.1
- UniProt
- O08452
- Ligands
- ZN, CA
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha amylase (EC 3.2.1.1) | protein | 434 | 31% helix, 24% strand | O08452 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.44 | 0.78 | 19 | empty |
| 2 | 79 | 0.33 | 0.74 | 18 | ZN |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1MWO · Crystal Structure Analysis of the Hyperthermostable Pyrocoocus woesei alpha-amylase · 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 O08452
- Elsewhere: RCSB PDB 1MWO · PDBe 1MWO · UniProt O08452
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