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2CAR

Crystal Structure Of Human Inosine Triphosphatase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006193biological_processITP catabolic process
A0009117biological_processnucleotide metabolic process
A0009143biological_processnucleoside triphosphate catabolic process
A0009204biological_processdeoxyribonucleoside triphosphate catabolic process
A0016787molecular_functionhydrolase activity
A0035870molecular_functiondITP diphosphatase activity
A0036220molecular_functionITP diphosphatase activity
A0036222molecular_functionXTP diphosphatase activity
A0042802molecular_functionidentical protein binding
A0043231cellular_componentintracellular membrane-bounded organelle
A0046872molecular_functionmetal ion binding
A0047429molecular_functionnucleoside triphosphate diphosphatase activity
A0051276biological_processchromosome organization
B0000166molecular_functionnucleotide binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006193biological_processITP catabolic process
B0009117biological_processnucleotide metabolic process
B0009143biological_processnucleoside triphosphate catabolic process
B0009204biological_processdeoxyribonucleoside triphosphate catabolic process
B0016787molecular_functionhydrolase activity
B0035870molecular_functiondITP diphosphatase activity
B0036220molecular_functionITP diphosphatase activity
B0036222molecular_functionXTP diphosphatase activity
B0042802molecular_functionidentical protein binding
B0043231cellular_componentintracellular membrane-bounded organelle
B0046872molecular_functionmetal ion binding
B0047429molecular_functionnucleoside triphosphate diphosphatase activity
B0051276biological_processchromosome organization
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:17138556, ECO:0007744|PDB:2J4E
ChainResidueDetails
ATHR14
BGLU44
BLYS56
BASP72
BLYS89
BPHE149
BLYS172
BHIS177
AGLU44
ALYS56
AASP72
ALYS89
APHE149
ALYS172
AHIS177
BTHR14

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000255|HAMAP-Rule:MF_03148, ECO:0000269|Ref.9
ChainResidueDetails
AALA2
BALA2

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PDB entries from 2024-09-04

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