Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6YMH

X-ray structure of the K72I, Y129F, R133L, H199A quadruple mutant of PNP-oxidase from E. coli in complex with PLP

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0004733molecular_functionpyridoxamine phosphate oxidase activity
AAA0005829cellular_componentcytosol
AAA0008615biological_processpyridoxine biosynthetic process
AAA0010181molecular_functionFMN binding
AAA0016491molecular_functionoxidoreductase activity
AAA0030170molecular_functionpyridoxal phosphate binding
AAA0032991cellular_componentprotein-containing complex
AAA0036001biological_process'de novo' pyridoxal 5'-phosphate biosynthetic process
AAA0042301molecular_functionphosphate ion binding
AAA0042803molecular_functionprotein homodimerization activity
AAA0042816biological_processvitamin B6 metabolic process
AAA0042823biological_processpyridoxal phosphate biosynthetic process
AAA1902444molecular_functionriboflavin binding
BBB0004733molecular_functionpyridoxamine phosphate oxidase activity
BBB0005829cellular_componentcytosol
BBB0008615biological_processpyridoxine biosynthetic process
BBB0010181molecular_functionFMN binding
BBB0016491molecular_functionoxidoreductase activity
BBB0030170molecular_functionpyridoxal phosphate binding
BBB0032991cellular_componentprotein-containing complex
BBB0036001biological_process'de novo' pyridoxal 5'-phosphate biosynthetic process
BBB0042301molecular_functionphosphate ion binding
BBB0042803molecular_functionprotein homodimerization activity
BBB0042816biological_processvitamin B6 metabolic process
BBB0042823biological_processpyridoxal phosphate biosynthetic process
BBB1902444molecular_functionriboflavin binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues17
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10903950","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11453690","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15858270","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11453690","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11786019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15858270","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15858270","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11786019","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 677
ChainResidueDetails

site_idMCSA2
Number of Residues1
DetailsM-CSA 677
ChainResidueDetails

239803

PDB entries from 2025-08-06

PDB statisticsPDBj update infoContact PDBjnumon