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Amylomaltase malq from escherichia COLI, apo structure

Analyse Amylomaltase malq from escherichia COLI, apo structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4S3P
Type: protein
Length: 1,380 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-alpha-glucanotransferase
EC: 2.4.1.25
UniProt: P15977
Pockets: 20 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-alpha-glucanotransferase (EC 2.4.1.25)	protein	691	44% helix, 17% strand	P15977
B	4-alpha-glucanotransferase (EC 2.4.1.25)	protein	689	43% helix, 18% strand	P15977

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1131	0.87	0.88	125	empty
2	128	0.81	0.98	26	empty
3	114	0.79	0.97	25	empty
4	84	0.74	0.97	26	empty
5	68	0.71	0.97	19	empty

Interfaces

1 interface between chains.

A–B · 2275 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

4S3P · Amylomaltase MalQ from Escherichia coli, apo structure · the same entry in another collection · chain A against A, TM-score 1.00
P15977 · AlphaFold monomer V2.0 prediction for 4-alpha-glucanotransferase (P15977) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P15977
Elsewhere: RCSB PDB 4S3P · PDBe 4S3P · UniProt P15977

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