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1ZWJ

X-ray structure of galt-like protein from arabidopsis thaliana AT5G18200

Replaces:  1VKV
Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0006006biological_processglucose metabolic process
A0006012biological_processgalactose metabolic process
A0008108molecular_functionUDP-glucose:hexose-1-phosphate uridylyltransferase activity
A0008270molecular_functionzinc ion binding
A0016779molecular_functionnucleotidyltransferase activity
A0017103molecular_functionUTP:galactose-1-phosphate uridylyltransferase activity
A0043531molecular_functionADP binding
A0046872molecular_functionmetal ion binding
A0047345molecular_functionribose-5-phosphate adenylyltransferase activity
A0080040biological_processpositive regulation of cellular response to phosphate starvation
B0005975biological_processcarbohydrate metabolic process
B0006006biological_processglucose metabolic process
B0006012biological_processgalactose metabolic process
B0008108molecular_functionUDP-glucose:hexose-1-phosphate uridylyltransferase activity
B0008270molecular_functionzinc ion binding
B0016779molecular_functionnucleotidyltransferase activity
B0017103molecular_functionUTP:galactose-1-phosphate uridylyltransferase activity
B0043531molecular_functionADP binding
B0046872molecular_functionmetal ion binding
B0047345molecular_functionribose-5-phosphate adenylyltransferase activity
B0080040biological_processpositive regulation of cellular response to phosphate starvation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
ACYS63
ACYS66
AHIS133
AHIS184

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS216
ACYS219
AHIS255
AHIS310

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BCYS66
BHIS133
BHIS184
BCYS63

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 403
ChainResidue
BCYS216
BCYS219
BHIS255
BHIS310

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-AMP-histidine intermediate => ECO:0000269|PubMed:16519510, ECO:0000269|PubMed:17850744
ChainResidueDetails
AHIS186
BHIS186

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|Ref.6
ChainResidueDetails
AARG41
BGLU72
BASN94
BASN173
BGLY179
BGLN188
BGLY321
BPHE325
AGLU72
AASN94
AASN173
AGLY179
AGLN188
AGLY321
APHE325
BARG41

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:16519510, ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6
ChainResidueDetails
ACYS63
BCYS66
BHIS133
BHIS184
BCYS216
BCYS219
BHIS255
BHIS310
ACYS66
AHIS133
AHIS184
ACYS216
ACYS219
AHIS255
AHIS310
BCYS63

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1hxq
ChainResidueDetails
AHIS186
AALA180
AHIS184
AGLN188

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1hxq
ChainResidueDetails
BHIS186
BALA180
BHIS184
BGLN188

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PDB entries from 2024-07-17

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