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1NVE

Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+ and NAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0003856molecular_function3-dehydroquinate synthase activity
A0005737cellular_componentcytoplasm
A0009073biological_processaromatic amino acid family biosynthetic process
A0016838molecular_functioncarbon-oxygen lyase activity, acting on phosphates
B0003856molecular_function3-dehydroquinate synthase activity
B0005737cellular_componentcytoplasm
B0009073biological_processaromatic amino acid family biosynthetic process
B0016838molecular_functioncarbon-oxygen lyase activity, acting on phosphates
C0003856molecular_function3-dehydroquinate synthase activity
C0005737cellular_componentcytoplasm
C0009073biological_processaromatic amino acid family biosynthetic process
C0016838molecular_functioncarbon-oxygen lyase activity, acting on phosphates
D0003856molecular_function3-dehydroquinate synthase activity
D0005737cellular_componentcytoplasm
D0009073biological_processaromatic amino acid family biosynthetic process
D0016838molecular_functioncarbon-oxygen lyase activity, acting on phosphates
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 600
ChainResidue
AASP146
AGLU194
AHIS271
AHIS287

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 601
ChainResidue
BASP146
BGLU194
BHIS271
BHIS287

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 602
ChainResidue
CGLU194
CHIS271
CHIS287
CASP146

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1603
ChainResidue
DASP146
DGLU194
DHIS271
DHIS287

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 604
ChainResidue
ALYS89
BLYS89

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 1605
ChainResidue
CLYS89
DLYS89
DHOH1686

site_idAC7
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NAD A 400
ChainResidue
AASP44
AASN46
AILE47
AGLU81
ALYS84
AGLY114
AGLY115
AVAL116
AASP119
ATHR139
ATHR140
AASP146
ASER147
ALYS152
AASN162
APHE179
ATHR182
ALEU183
APRO184
AGLU187
AHOH714
AHOH732
AHOH759

site_idAC8
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD B 401
ChainResidue
BASP44
BASN46
BILE47
BGLU81
BLYS84
BGLY114
BGLY115
BVAL116
BASP119
BTHR139
BTHR140
BASP146
BSER147
BLYS152
BASN162
BPHE179
BTHR182
BLEU183
BPRO184
BGLU187
BHOH607
BHOH608
BHOH638
BHOH647
BHOH663
BHOH727

site_idAC9
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NAD C 402
ChainResidue
CASP44
CASN46
CILE47
CGLU81
CLYS84
CGLY114
CGLY115
CVAL116
CASP119
CTHR139
CTHR140
CLEU142
CASP146
CSER147
CLYS152
CPHE179
CTHR182
CLEU183
CGLU187
CHOH1608
CHOH1616
CHOH1618
CHOH1735

site_idBC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAD D 1403
ChainResidue
DGLY115
DVAL116
DASP119
DTHR139
DTHR140
DASP146
DSER147
DLYS152
DASN162
DPHE179
DTHR182
DLEU183
DPRO184
DGLU187
DHOH1626
DHOH1698
DASP44
DASN46
DILE47
DGLU81
DLYS84
DGLY114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton acceptor; for 3-dehydroquinate synthase activity
ChainResidueDetails
AGLU260
AHIS275
BGLU260
BHIS275
CGLU260
CHIS275
DGLU260
DHIS275

site_idSWS_FT_FI2
Number of Residues44
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03143, ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163
ChainResidueDetails
AASP44
AHIS271
AHIS287
BASP44
BGLU81
BGLY114
BASP119
BTHR139
BLYS161
BPHE179
BASN190
AGLU81
BGLU194
BHIS271
BHIS287
CASP44
CGLU81
CGLY114
CASP119
CTHR139
CLYS161
CPHE179
AGLY114
CASN190
CGLU194
CHIS271
CHIS287
DASP44
DGLU81
DGLY114
DASP119
DTHR139
DLYS161
AASP119
DPHE179
DASN190
DGLU194
DHIS271
DHIS287
ATHR139
ALYS161
APHE179
AASN190
AGLU194

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING:
ChainResidueDetails
AARG130
BLYS152
BASN162
BLYS250
BARG264
BLYS356
CARG130
CASP146
CLYS152
CASN162
CLYS250
AASP146
CARG264
CLYS356
DARG130
DASP146
DLYS152
DASN162
DLYS250
DARG264
DLYS356
ALYS152
AASN162
ALYS250
AARG264
ALYS356
BARG130
BASP146

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqs
ChainResidueDetails
AHIS275

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqs
ChainResidueDetails
BHIS275

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqs
ChainResidueDetails
CHIS275

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqs
ChainResidueDetails
DHIS275

site_idMCSA1
Number of Residues10
DetailsM-CSA 59
ChainResidueDetails
AARG130electrostatic stabiliser
AHIS287metal ligand
ALYS152hydrogen bond donor, steric role
AGLU194metal ligand
ALYS250electrostatic stabiliser, hydrogen bond donor, steric role
AGLU260hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AARG264electrostatic stabiliser, hydrogen bond donor, steric role
AASN268hydrogen bond donor, steric role
AHIS271metal ligand
AHIS275hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues10
DetailsM-CSA 59
ChainResidueDetails
BARG130electrostatic stabiliser
BHIS287metal ligand
BLYS152hydrogen bond donor, steric role
BGLU194metal ligand
BLYS250electrostatic stabiliser, hydrogen bond donor, steric role
BGLU260hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BARG264electrostatic stabiliser, hydrogen bond donor, steric role
BASN268hydrogen bond donor, steric role
BHIS271metal ligand
BHIS275hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA3
Number of Residues10
DetailsM-CSA 59
ChainResidueDetails
CARG130electrostatic stabiliser
CHIS287metal ligand
CLYS152hydrogen bond donor, steric role
CGLU194metal ligand
CLYS250electrostatic stabiliser, hydrogen bond donor, steric role
CGLU260hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
CARG264electrostatic stabiliser, hydrogen bond donor, steric role
CASN268hydrogen bond donor, steric role
CHIS271metal ligand
CHIS275hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA4
Number of Residues10
DetailsM-CSA 59
ChainResidueDetails
DARG130electrostatic stabiliser
DHIS287metal ligand
DLYS152hydrogen bond donor, steric role
DGLU194metal ligand
DLYS250electrostatic stabiliser, hydrogen bond donor, steric role
DGLU260hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
DARG264electrostatic stabiliser, hydrogen bond donor, steric role
DASN268hydrogen bond donor, steric role
DHIS271metal ligand
DHIS275hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-10-30

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