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4DY6

Crystal structure of NAD kinase 1 from Listeria monocytogenes in complex with 2'-phosphate bis(adenosine)-5'-diphosphate

Replaces:  2I2E
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 Residues20
DetailsBINDING SITE FOR RESIDUE A22 A 301
ChainResidue
AASP45
ATHR161
AALA162
ATYR163
ASER166
AALA185
AILE187
AHIS223
AHOH437
AHOH442
AHOH444
AGLY46
AHOH449
AHIS71
APHE74
ATYR75
AASN122
AGLU123
AASP150
ASER158

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CIT A 302
ChainResidue
AVAL98
ATYR100
AHIS173
APHE251
APRO252
APHE253
AARG256
AHOH452
AHOH494

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
AASP45

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
ChainResidueDetails
AGLY46
AASN122
ASER158
ATHR161
AHIS223
AASP45

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

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PDB entries from 2024-04-17

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