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Crystal structure of L,L-diaminopimelate aminotransferase (dapl) from verrucomicrobium spinosum

Analyse Crystal structure of L,L-diaminopimelate aminotransferase (dapl) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6OXM
Type
protein
Length
808 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Diaminopimelate aminotransferase
EC
2.6.1.83
Pockets
9 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BDiaminopimelate aminotransferase (EC 2.6.1.83)protein40445% helix, 16% strand—

Pockets

9 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17240.780.8268empty
27500.770.8164empty
3900.760.9823empty
4720.740.9922empty
51980.640.8428empty

Interfaces

1 interface between chains.

  • A–B · 3371 Ų buried · 58 hydrogen bonds · protein-protein

Compared structures

  • 6OXM · Crystal structure of L,L-diaminopimelate aminotransferase (DapL) from Verrucomicrobium… · the same entry in another collection · chain A against A, TM-score 1.00

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