Research workbench

Mate transporter norm-ng in complex with cs+ and monobody

Analyse Mate transporter norm-ng in complex with cs+ and monobody in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HUL
Type: protein
Length: 550 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Multidrug efflux protein; Protein B
UniProt: E8SM44
Ligands: CS
Pockets: 6 · best druggability 0.89

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Multidrug efflux protein	protein	459	36% helix, 0% strand	E8SM44
B	Protein B	protein	91	0% helix, 31% strand	—

Ligands and binding sites

CS · Cesium ion · metal · chains A

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

Pockets

6 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	1173	0.89	0.90	146	CS
2	84	0.65	0.91	22	empty
3	120	0.60	0.85	30	empty
4	97	0.46	0.80	18	empty
5	125	0.43	0.76	21	empty

Interfaces

1 interface between chains.

A–B · 509 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4HUL · MATE transporter NorM-NG in complex with Cs+ and monobody · 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 E8SM44
Elsewhere: RCSB PDB 4HUL · PDBe 4HUL · UniProt E8SM44

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