Research workbench
Crystal structure analysis of the complex between psychrophilic alpha amylase from pseudoalteromonas haloplanctis and nitrate
Analyse Crystal structure analysis of the complex between psychrophilic alpha amylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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