MolNFT v1 · #31763 · protein

Crystal structure of the novel alpha-amylase amyc from thermotoga maritima

2B5D: “Crystal structure of the novel alpha-amylase amyc from thermotoga maritima”. X-ray diffraction, 4 pockets (best druggability 0.74). MolNFT v1 #31763 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2B5D
Type: protein
Length: 518 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-amylase
EC: 3.2.1.1
Pockets: 4 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Alpha-amylase (EC 3.2.1.1)	protein	518	54% helix, 10% strand	—

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	535	0.74	0.82	86	empty
2	137	0.65	0.87	21	empty
3	152	0.50	0.78	20	empty
4	80	0.41	0.79	22	empty

Compared structures

2B5D · Crystal structure of the novel alpha-amylase AmyC from Thermotoga maritima · the same entry in another collection · chain X against X, 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 2B5D · PDBe 2B5D

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