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Refined structures of two INSERTION(SLASH)DELETION mutants probe function of the maltodextrin binding protein

Analyse Refined structures of two INSERTION(SLASH)DELETION mutants probe function of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MDP
Type: protein
Length: 726 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Maltodextrin binding protein
UniProt: P02928
Ligands: GLC
Pockets: 4 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
1, 2	Maltodextrin binding protein	protein	363	41% helix, 20% strand	P02928

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 4 copies · chains 1, 2

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 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	1116	0.83	0.84	98	GLC
2	84	0.37	0.76	19	empty
3	67	0.31	0.74	18	empty
4	64	0.29	0.74	16	empty

Interfaces

1 interface between chains.

1–2 · 447 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

1MDP · Refined structures of two INSERTION(SLASH)DELETION mutants probe function of the… · the same entry in another collection · chain 1 against 1, 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 P02928
Elsewhere: RCSB PDB 1MDP · PDBe 1MDP · UniProt P02928

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