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1IFX

CRYSTAL STRUCTURE OF NH3-DEPENDENT NAD+ SYNTHETASE FROM BACILLUS SUBTILIS COMPLEXED WITH TWO MOLECULES DEAMIDO-NAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0003952molecular_functionNAD+ synthase (glutamine-hydrolyzing) activity
A0004359molecular_functionglutaminase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008795molecular_functionNAD+ synthase activity
A0009435biological_processNAD biosynthetic process
A0016874molecular_functionligase activity
A0030435biological_processsporulation resulting in formation of a cellular spore
A0046872molecular_functionmetal ion binding
B0003952molecular_functionNAD+ synthase (glutamine-hydrolyzing) activity
B0004359molecular_functionglutaminase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0008795molecular_functionNAD+ synthase activity
B0009435biological_processNAD biosynthetic process
B0016874molecular_functionligase activity
B0030435biological_processsporulation resulting in formation of a cellular spore
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE DND B 7000
ChainResidue
ATYR32
BPHE1168
BTHR1169
BLYS1170
BASP1173
BHIS1257
BLYS1258
BHOH6091
BHOH6181
BHOH6214
ATHR36
ATYR144
ALEU153
AASP177
BPHE1129
BASN1133
BARG1137
BPHE1167

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE DND A 8000
ChainResidue
APHE129
AASN133
AARG137
APHE167
APHE168
ATHR169
ALYS170
AHIS257
ALYS258
AHOH6022
AHOH6171
AHOH6215
BTYR1032
BTHR1036
BTYR1144
BLEU1153
BASP1177

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1IFX, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:2NSY
ChainResidueDetails
AVAL33
BVAL1033

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193, ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1FYD, ECO:0007744|PDB:1IH8, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY
ChainResidueDetails
AILE45
AARG187
BILE1045
BARG1187

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY
ChainResidueDetails
ASER51
AALA163
BSER1051
BALA1163

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1FYD, ECO:0007744|PDB:1IH8, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY
ChainResidueDetails
ALEU79
AGLN85
BLEU1079
BGLN1085

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00193, ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1IFX, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:2NSY
ChainResidueDetails
ATHR138
ATYR171
ALYS258
BTHR1138
BTYR1171
BLYS1258

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193, ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY
ChainResidueDetails
AASP158
BASP1158

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193, ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1IFX, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:2NSY
ChainResidueDetails
ALEU178
BLEU1178

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193, ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1FYD, ECO:0007744|PDB:1IH8, ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY
ChainResidueDetails
AALA209
BALA1209

site_idSWS_FT_FI9
Number of Residues2
DetailsBINDING: in other chain => ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:2NSY
ChainResidueDetails
ALEU224
BLEU1224

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 200
ChainResidueDetails
ASER51metal ligand
AALA163metal ligand

site_idMCSA2
Number of Residues2
DetailsM-CSA 200
ChainResidueDetails
BSER1051metal ligand
BALA1163metal ligand

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PDB entries from 2024-05-01

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