MolNFT v1 · #165252 · protein

Crystal structure of bacillus paralicheniformis alpha-amylase in complex with maltotetraose

6TP1: “Crystal structure of bacillus paralicheniformis alpha-amylase in complex with maltotetraose”. X-ray diffraction, 3 ligands (GLC, CA, NA), 3 pockets (best druggability 0.51). MolNFT v1 #165252 on GenesisL1: 3D structure, binding…

PDB: 6TP1
Type: protein
Length: 481 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amylase
EC: 3.2.1.1
UniProt: I3P686
Ligands: GLC, CA, NA
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amylase (EC 3.2.1.1)	protein	481	27% helix, 25% strand	I3P686

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A
CA · Calcium ion · metal · 2 copies · chains A
NA · Sodium ion · metal · 2 copies · chains A
ACY · Acetic acid · additive · 2 copies · chains A
MLI · Malonate ion · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	159	0.51	0.79	25	MLI
2	52	0.41	0.82	14	empty
3	68	0.28	0.73	22	GLC

Compared structures

6TP1 · Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with… · 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
Every structure of UniProt I3P686
Elsewhere: RCSB PDB 6TP1 · PDBe 6TP1 · UniProt I3P686

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