MolNFT v1 · #109873 · protein

Crystal structure of leucine-, isoleucine-, valine-, threonine-, and alanine-binding protein from brucella ovis

4XFK · Putative branched chain amino acid ABC transporter…: “Crystal structure of leucine-, isoleucine-, valine-, threonine-, and alanine-binding protein from brucella…”. X-ray diffraction, 1 ligand (NA), 4 pockets (best druggability…

PDB: 4XFK
Type: protein
Length: 391 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative branched chain amino acid ABC transporter, periplasmic amino acid-binding protein
UniProt: A5VTF2
Ligands: NA
Pockets: 4 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative branched chain amino acid ABC transporter, periplasmic amino acid-binding protein	protein	391	42% helix, 20% strand	A5VTF2

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains A
ACT · Acetate ion · additive · 2 copies · chains A

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

Pockets

4 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	118	0.60	0.85	23	empty
2	175	0.53	0.79	29	empty
3	84	0.41	0.78	15	empty
4	50	0.24	0.72	12	empty

Compared structures

4XFK · Crystal structure of Leucine-, Isoleucine-, Valine-, Threonine-, and Alanine-binding… · 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 A5VTF2
Elsewhere: RCSB PDB 4XFK · PDBe 4XFK · UniProt A5VTF2

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