MolNFT v1 · #80242 · protein

Structure of a ABC transporter, periplasmic substrate-binding protein from coxiella burnetii

3TQW · Methionine-binding protein: “Structure of a ABC transporter, periplasmic substrate-binding protein from coxiella burnetii”. X-ray diffraction, 2 ligands (MET, SO4), 3 pockets (best druggability 0.76). MolNFT v1 #80242 on GenesisL1…

PDB: 3TQW
Type: protein
Length: 468 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methionine-binding protein
UniProt: Q83F42
Ligands: MET, SO4
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methionine-binding protein	protein	235	40% helix, 26% strand	Q83F42
B	Methionine-binding protein	protein	233	39% helix, 25% strand	Q83F42

Ligands and binding sites

MET · Methionine · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · chains B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	433	0.76	0.85	63	empty
2	436	0.61	0.76	56	empty
3	178	0.47	0.75	22	empty

Interfaces

1 interface between chains.

A–B · 890 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

3TQW · Structure of a ABC transporter, periplasmic substrate-binding protein from Coxiella… · 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 Q83F42
Elsewhere: RCSB PDB 3TQW · PDBe 3TQW · UniProt Q83F42

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