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

2VU5

Crystal structure of Pndk from Bacillus anthracis

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
A0009142biological_processnucleoside triphosphate biosynthetic process
A0016301molecular_functionkinase activity
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00469
Number of Residues9
DetailsNDPK Nucleoside diphosphate kinase (NDPK) active site signature. NiiHGSDSL
ChainResidueDetails
AASN112-LEU120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Pros-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_00451
ChainResidueDetails
AHIS115

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00451
ChainResidueDetails
ALYS9
APHE57
AARG85
ATHR91
AARG102
AASN112

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000255|HAMAP-Rule:MF_00451
ChainResidueDetails
ATHR91

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000255|HAMAP-Rule:MF_00451
ChainResidueDetails
ASER122

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
ATYR49
ALYS9

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon