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

3V8Q

Crystal structure of NAD kinase 1 H223E mutant from Listeria monocytogenes in complex with 5'-amino-5'-deoxyadenosine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003951molecular_functionNAD+ kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006741biological_processNADP biosynthetic process
A0016301molecular_functionkinase activity
A0019674biological_processNAD metabolic process
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 5N5 A 301
ChainResidue
AASN122
AASP222
AGLU123
AGLY149
AASP150
AALA162
ATYR163
ASER166
AALA185
AILE187

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
AASP45
APHE74
AASN122
ASER158
ATHR161
AALA162

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CIT A 303
ChainResidue
ATYR100
AHIS173
AARG247
APHE251
APRO252
APHE253
AARG256
AHOH422
AHOH426

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
AGLU223
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

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon