GL1X · GenesisL1 explorer

Research workbench

Crystal structure of a domain of transmembrane protein of ABC-type oligopeptide transport system from bartonella henselae str. houston-1

Analyse Crystal structure of a domain of transmembrane protein of ABC-type oligopeptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3PAM
Type
protein
Length
506 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transmembrane protein
UniProt
Q6G3A9
Pockets
3 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATransmembrane proteinprotein25643% helix, 15% strandQ6G3A9
BTransmembrane proteinprotein25044% helix, 15% strandQ6G3A9

Ligands and binding sites

  • EOH · Ethanol · additive · 10 copies · chains A, 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11410.590.8425empty
2770.500.8420empty
3760.360.7720empty

Interfaces

1 interface between chains.

  • A–B · 508 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

  • 3PAM · Crystal structure of a domain of transmembrane protein of ABC-type oligopeptide transport… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.