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

1WKL

Crystal Structure of Nucleoside Diphosphate Kinase from Thermus thermophilus HB8 in Complex with ATP and ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006183biological_processGTP biosynthetic process
A0006228biological_processUTP biosynthetic process
A0006241biological_processCTP biosynthetic process
A0009117biological_processnucleotide metabolic process
A0016301molecular_functionkinase activity
A0046872molecular_functionmetal ion binding
B0004550molecular_functionnucleoside diphosphate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006183biological_processGTP biosynthetic process
B0006228biological_processUTP biosynthetic process
B0006241biological_processCTP biosynthetic process
B0009117biological_processnucleotide metabolic process
B0016301molecular_functionkinase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 900
ChainResidue
BARG85
BMET88
BARG102
BHIS115
BGLY116
BATP856

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PHS A 138
ChainResidue
ATYR49
AHIS115
AADP646
AMET7
ALYS9
AHIS48

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ADP A 646
ChainResidue
ALYS9
ATYR49
AHIS52
APHE57
AARG85
ATHR91
AARG102
AILE109
AASP110
AASN112
APHS138

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ATP B 856
ChainResidue
BLYS9
BHIS52
BPHE57
BLEU61
BARG85
BTHR91
BILE109
BASP110
BHIS115
BMG900
BHOH927

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Pros-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_00451
ChainResidueDetails
AHIS115
BHIS115

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00451, ECO:0000269|PubMed:14501133
ChainResidueDetails
ALYS9
BTHR91
BARG102
BASN112
APHE57
AARG85
ATHR91
AARG102
AASN112
BLYS9
BPHE57
BARG85

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
AASN112
ALYS9

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
BASN112
BLYS9

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
ATYR49
ALYS9

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
BTYR49
BLYS9

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon