MolNFT v1 · #1080 · protein
Alpha-amylase from alteromonas haloplanctis complexed with tris
1AQM: “Alpha-amylase from alteromonas haloplanctis complexed with tris”. X-ray diffraction, 2 ligands (CA, CL), 2 pockets (best druggability 0.62). MolNFT v1 #1080 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1AQM
- Type
- protein
- Length
- 448 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-amylase
- EC
- 3.2.1.1
- UniProt
- P29957
- Ligands
- CA, CL
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-amylase (EC 3.2.1.1) | protein | 448 | 31% helix, 23% strand | P29957 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 304 | 0.62 | 0.79 | 23 | TRS |
| 2 | 84 | 0.35 | 0.75 | 19 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 P29957
- Elsewhere: RCSB PDB 1AQM · PDBe 1AQM · UniProt P29957
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