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

2YVU

Crystal structure of APE1195

Functional Information from GO Data
ChainGOidnamespacecontents
A0000103biological_processsulfate assimilation
A0000166molecular_functionnucleotide binding
A0004020molecular_functionadenylylsulfate kinase activity
A0004781molecular_functionsulfate adenylyltransferase (ATP) activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0010134biological_processsulfate assimilation via adenylyl sulfate reduction
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0019379biological_processsulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
A0070814biological_processhydrogen sulfide biosynthetic process
B0000103biological_processsulfate assimilation
B0000166molecular_functionnucleotide binding
B0004020molecular_functionadenylylsulfate kinase activity
B0004781molecular_functionsulfate adenylyltransferase (ATP) activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0010134biological_processsulfate assimilation via adenylyl sulfate reduction
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0019379biological_processsulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
B0070814biological_processhydrogen sulfide biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Phosphoserine intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon