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Crystal structure of the E257A mutant of BLMAN5B in complex with glcnac (co-crystallization)

Analyse Crystal structure of the E257A mutant of BLMAN5B in complex with glcnac… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MOY
Type: protein
Length: 850 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BLMAN5B
UniProt: B3DQP5
Ligands: NAG
Pockets: 7 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BLMAN5B	protein	424	41% helix, 15% strand	B3DQP5
B	BLMAN5B	protein	426	41% helix, 15% strand	B3DQP5

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B

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

Pockets

7 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	194	0.83	0.97	32	NAG
2	196	0.82	0.96	44	empty
3	179	0.81	0.96	31	NAG
4	61	0.44	0.83	19	empty
5	56	0.37	0.79	19	empty

Interfaces

1 interface between chains.

A–B · 1831 Å² buried · 31 hydrogen bonds · protein-protein

Compared structures

6MOY · Crystal structure of the E257A mutant of BlMan5B in complex with GlcNAc… · 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 B3DQP5
Elsewhere: RCSB PDB 6MOY · PDBe 6MOY · UniProt B3DQP5

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