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Crystal structure of lipoylated E. COLI H-protein (reduced form)

Analyse Crystal structure of lipoylated E. COLI H-protein (reduced form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3AB9
Type
protein
Length
127 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycine cleavage system H protein
UniProt
P0A6T9
Ligands
CA, CL

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycine cleavage system H proteinprotein12724% helix, 34% strandP0A6T9

Ligands and binding sites

  • CA · Calcium ion · metal · chains A
  • CL · Chloride ion · ion · chains A

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

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

  • 3AB9 · Crystal Structure of lipoylated E. coli H-protein (reduced form) · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A6T9 · AlphaFold monomer V2.0 prediction for glycine cleavage system H protein (P0A6T9) · a predicted model of the same protein · chain A against A, TM-score 0.99

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