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5IN3

Crystal structure of glucose-1-phosphate bound nucleotidylated human galactose-1-phosphate uridylyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006011biological_processUDP-glucose metabolic process
A0006012biological_processgalactose metabolic process
A0008108molecular_functionUDP-glucose:hexose-1-phosphate uridylyltransferase activity
A0008270molecular_functionzinc ion binding
A0016779molecular_functionnucleotidyltransferase activity
A0033499biological_processgalactose catabolic process via UDP-galactose
A0046872molecular_functionmetal ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0006011biological_processUDP-glucose metabolic process
B0006012biological_processgalactose metabolic process
B0008108molecular_functionUDP-glucose:hexose-1-phosphate uridylyltransferase activity
B0008270molecular_functionzinc ion binding
B0016779molecular_functionnucleotidyltransferase activity
B0033499biological_processgalactose catabolic process via UDP-galactose
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00117
Number of Residues18
DetailsGAL_P_UDP_TRANSF_I Galactose-1-phosphate uridyl transferase family 1 active site signature. FENKGammGcsnpHPHcQ
ChainResidueDetails
BPHE171-GLN188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-UMP-histidine intermediate => ECO:0000255|PROSITE-ProRule:PRU10033, ECO:0000269|PubMed:27005423
ChainResidueDetails
BHIS186
AHIS186

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10033
ChainResidueDetails
BCYS75
BHIS184
ACYS75
AHIS184

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: in other chain => ECO:0000305|PubMed:27005423
ChainResidueDetails
BALA81
ATYR339
BASN97
BGLN188
BLYS334
BTYR339
AALA81
AASN97
AGLN188
ALYS334

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:27005423
ChainResidueDetails
BASN173
AASN173

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:27005423
ChainResidueDetails
BGLU202
BHIS301
BHIS319
BHIS321
AGLU202
AHIS301
AHIS319
AHIS321

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PDB entries from 2024-11-06

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