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The structure of mbp-MCL1 bound to ligand 6 at 2.0A

Analyse The structure of mbp-MCL1 bound to ligand 6 at 2.0A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WMX
Type: protein
Length: 516 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mbp-MCL1 chimera protein
UniProt: P0AEX9, Q07820
Ligands: 3R7, GLC, MG
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mbp-MCL1 chimera protein	protein	516	55% helix, 14% strand	P0AEX9, Q07820

Ligands and binding sites

3R7 · 4-ethenyl-2-[(phenylsulfonyl)amino]benzoic acid · ligand · chains A
GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
MG · Magnesium ion · metal · chains A
FMT · Formic acid · additive · 10 copies · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	222	0.70	0.86	30	GLC
2	480	0.67	0.79	47	FMT
3	111	0.51	0.80	19	3R7

Compared structures

4WMX · The structure of MBP-MCL1 bound to ligand 6 at 2.0A · 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 P0AEX9
Every structure of UniProt Q07820
Elsewhere: RCSB PDB 4WMX · PDBe 4WMX · UniProt P0AEX9 · UniProt Q07820

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