MolNFT v1 · #23993 · protein

Thermoactinomyces vulgaris R-47 alpha-amylase 1/MALTO-tridecaose complex

1UH4 · Alpha-amylase I: “Thermoactinomyces vulgaris R-47 alpha-amylase 1/MALTO-tridecaose complex”. X-ray diffraction, 3 ligands (GLC, BGC, CA), 3 pockets (best druggability 0.68). MolNFT v1 #23993 on GenesisL1: 3D structure, binding sites…

PDB: 1UH4
Type: protein
Length: 637 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-amylase I
EC: 3.2.1.1
Ligands: GLC, BGC, CA
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-amylase I (EC 3.2.1.1)	protein	637	24% helix, 27% strand	—

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 16 copies · chains A
BGC · beta-D-glucopyranose · sugar · 2 copies · chains A
CA · Calcium ion · metal · 3 copies · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	243	0.68	0.85	40	MPD
2	255	0.55	0.77	34	GLC
3	73	0.34	0.75	17	empty

Compared structures

1UH4 · Thermoactinomyces vulgaris R-47 alpha-amylase 1/malto-tridecaose complex · 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
Elsewhere: RCSB PDB 1UH4 · PDBe 1UH4

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