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Crystal structure of serine dehydrogenase from escherichia COLI

Analyse Crystal structure of serine dehydrogenase from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ASU
Type
protein
Length
434 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Short-chain DEHYDROGENASE/REDUCTASE sdr
EC
1.1.1.276
Pockets
4 · best druggability 0.48

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AShort-chain DEHYDROGENASE/REDUCTASE sdr (EC 1.1.1.276)protein21845% helix, 17% strand—
BShort-chain DEHYDROGENASE/REDUCTASE sdr (EC 1.1.1.276)protein21645% helix, 16% strand—

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11310.480.7920empty
21750.460.7527empty
31000.440.7918empty
41450.410.7429empty

Interfaces

1 interface between chains.

  • A–B · 1809 Ų buried · 35 hydrogen bonds · protein-protein

Compared structures

  • 3ASU · Crystal structure of serine dehydrogenase from Escherichia coli · the same entry in another collection · chain B against B, TM-score 1.00

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