Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1NHK

CRYSTAL STRUCTURE OF MYXOCOCCUS XANTHUS NUCLEOSIDE DIPHOSPHATE KINASE AND ITS INTERACTION WITH A NUCLEOTIDE SUBSTRATE AT 2.0 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
L0000166molecular_functionnucleotide binding
L0004550molecular_functionnucleoside diphosphate kinase activity
L0005524molecular_functionATP binding
L0005737cellular_componentcytoplasm
L0006183biological_processGTP biosynthetic process
L0006228biological_processUTP biosynthetic process
L0006241biological_processCTP biosynthetic process
L0009117biological_processnucleotide metabolic process
L0009142biological_processnucleoside triphosphate biosynthetic process
L0016301molecular_functionkinase activity
L0016310biological_processphosphorylation
L0016740molecular_functiontransferase activity
L0046872molecular_functionmetal ion binding
R0000166molecular_functionnucleotide binding
R0004550molecular_functionnucleoside diphosphate kinase activity
R0005524molecular_functionATP binding
R0005737cellular_componentcytoplasm
R0006183biological_processGTP biosynthetic process
R0006228biological_processUTP biosynthetic process
R0006241biological_processCTP biosynthetic process
R0009117biological_processnucleotide metabolic process
R0009142biological_processnucleoside triphosphate biosynthetic process
R0016301molecular_functionkinase activity
R0016310biological_processphosphorylation
R0016740molecular_functiontransferase activity
R0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CMP R 1
ChainResidue
RLYS11
RTYR51
RPHE59
RLEU63
RILE111
RASN114
RHIS117
RHOH156

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CMP L 146
ChainResidue
LTYR51
LHIS54
LPHE59
LLEU63
LILE111
LASN114
LHIS117
LHOH160
LHOH194
LLYS11

Functional Information from PROSITE/UniProt
site_idPS00469
Number of Residues9
DetailsNDP_KINASES Nucleoside diphosphate kinases active site. NtvHGSDSL
ChainResidueDetails
RASN114-LEU122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Pros-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_00451
ChainResidueDetails
RGLY118
LGLY118

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00451
ChainResidueDetails
RPRO12
LASN94
LLYS105
LTHR115
RPHE60
RASP88
RASN94
RLYS105
RTHR115
LPRO12
LPHE60
LASP88

217705

PDB entries from 2024-03-27

PDB statisticsPDBj update infoContact PDBjnumon