MolNFT v1 · #13085 · protein
Crystal structure analysis of the complex between psychrophilic alpha amylase from pseudoalteromonas haloplanctis and nitrate
1L0P · Alpha-amylase: “Crystal structure analysis of the complex between psychrophilic alpha amylase from pseudoalteromonas…”. X-ray diffraction, 2 ligands (CA, NO3), 3 pockets (best druggability 0.62). MolNFT v1 #13085 on GenesisL1: 3D…
- PDB
- 1L0P
- 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, NO3
- Pockets
- 3 · 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
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 312 | 0.62 | 0.79 | 27 | empty |
| 2 | 94 | 0.37 | 0.76 | 20 | empty |
| 3 | 52 | 0.30 | 0.76 | 15 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1L0P · Crystal structure analysis of the complex between psychrophilic alpha amylase from… · the same entry in another collection · chain A against A, TM-score 1.00
- P29957 · AlphaFold monomer V2.0 prediction for alpha-amylase (P29957) · a predicted model of the same protein · 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 P29957
- Elsewhere: RCSB PDB 1L0P · PDBe 1L0P · UniProt P29957
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