MolNFT v1 · #11122 · protein

Crystal structure analysis of the mutant K300Q of pseudoalteromonas haloplanctis alpha-amylase

1JD9: “Crystal structure analysis of the mutant K300Q of pseudoalteromonas haloplanctis alpha-amylase”. X-ray diffraction, 1 ligand (CA), 3 pockets (best druggability 0.61). MolNFT v1 #11122 on GenesisL1: 3D structure, binding sites and…

PDB: 1JD9
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
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-amylase (EC 3.2.1.1)	protein	448	31% helix, 22% strand	P29957

Ligands and binding sites

CA · Calcium ion · metal · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	299	0.61	0.79	24	empty
2	99	0.37	0.76	20	empty
3	56	0.31	0.76	16	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1JD9 · Crystal structure analysis of the mutant K300Q of pseudoalteromonas haloplanctis… · 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 1JD9 · PDBe 1JD9 · UniProt P29957

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.