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2I2F

Crystal structure of LmNADK1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003951molecular_functionNAD+ kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006741biological_processNADP biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0019674biological_processNAD metabolic process
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 273
ChainResidue
AASN45
AGLY46
ANAD274

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NAD A 274
ChainResidue
AASP150
ATHR161
AALA162
ATYR163
ASER166
AALA185
AILE187
ATYR192
AHIS223
APO4273
AASN45
APHE74
ATYR75
AASN122
AGLU123
APRO132

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
AHIS173
AHIS205
APRO252
APHE253

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
ChainResidueDetails
AASN45

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
ChainResidueDetails
AASN45
AGLY46
AASN122
ASER158
ATHR161
AHIS223

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361
ChainResidueDetails
AARG148

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:17686780
ChainResidueDetails
AASP150

218853

PDB entries from 2024-04-24

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