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Structure of a bacterial metal transporter

Analyse Structure of a bacterial metal transporter in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BTX
Type: protein
Length: 377 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Solute carrier family 39 (iron-regulated transporter)
UniProt: Q6MLJ0
Ligands: EDT, CA, NI
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Solute carrier family 39 (iron-regulated transporter)	protein	377	82% helix, 0% strand	Q6MLJ0

Ligands and binding sites

EDT · {[-(bis-carboxymethyl-amino)-ethyl]-carboxymethyl-amino}-acetic acid · ligand · chains A
CA · Calcium ion · metal · chains A
NI · Nickel (II) ion · metal · chains A
OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	645	0.70	0.78	56	EDT, NI
2	55	0.28	0.73	12	empty
3	61	0.26	0.72	11	empty

Compared structures

6BTX · Structure of a bacterial metal transporter · 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 Q6MLJ0
Elsewhere: RCSB PDB 6BTX · PDBe 6BTX · UniProt Q6MLJ0

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