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1Z9D

Crystal structure of a putative uridylate kinase (UMP-kinase) from Streptococcus pyogenes

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006225biological_processUDP biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0033862molecular_functionUMP kinase activity
A0044210biological_process'de novo' CTP biosynthetic process
A0046940biological_processnucleoside monophosphate phosphorylation
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006225biological_processUDP biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0033862molecular_functionUMP kinase activity
B0044210biological_process'de novo' CTP biosynthetic process
B0046940biological_processnucleoside monophosphate phosphorylation
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006221biological_processpyrimidine nucleotide biosynthetic process
C0006225biological_processUDP biosynthetic process
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0033862molecular_functionUMP kinase activity
C0044210biological_process'de novo' CTP biosynthetic process
C0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1001
ChainResidue
AARG101
AARG119
AARG128
BARG122
BHOH1024

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1002
ChainResidue
BHOH1014
CARG122
BARG101
BARG119
BHIS123
BARG128

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
AARG119
AARG122
CARG101
CARG119

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1004
ChainResidue
ASER15
ALYS163
AASN164

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1005
ChainResidue
BSER15
BLYS163
BASN164
BHOH1040

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 1006
ChainResidue
CSER15
CLYS163
CASN164
CHOH1034

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1007
ChainResidue
ALYS13
ASER15
AGLY16
AGLY54
AGLY55
ATHR143
AHOH1024

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1008
ChainResidue
BSER15
BGLY16
BGLY54
BGLY55
BTHR143
BHOH1015

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 1009
ChainResidue
CLYS13
CSER15
CGLY54
CGLY55
CTHR143
CHOH1033

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsRegion: {"description":"Involved in allosteric activation by GTP","evidences":[{"source":"HAMAP-Rule","id":"MF_01220","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues51
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01220","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242199

PDB entries from 2025-09-24

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