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6HSU

The crystal structure of type II Dehydroquinase from Psychromonas ingrahamii 37, crystal form 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0003855molecular_function3-dehydroquinate dehydratase activity
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
A0016829molecular_functionlyase activity
B0003855molecular_function3-dehydroquinate dehydratase activity
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0009423biological_processchorismate biosynthetic process
B0016829molecular_functionlyase activity
C0003855molecular_function3-dehydroquinate dehydratase activity
C0008652biological_processamino acid biosynthetic process
C0009073biological_processaromatic amino acid family biosynthetic process
C0009423biological_processchorismate biosynthetic process
C0016829molecular_functionlyase activity
D0003855molecular_function3-dehydroquinate dehydratase activity
D0008652biological_processamino acid biosynthetic process
D0009073biological_processaromatic amino acid family biosynthetic process
D0009423biological_processchorismate biosynthetic process
D0016829molecular_functionlyase activity
E0003855molecular_function3-dehydroquinate dehydratase activity
E0008652biological_processamino acid biosynthetic process
E0009073biological_processaromatic amino acid family biosynthetic process
E0009423biological_processchorismate biosynthetic process
E0016829molecular_functionlyase activity
F0003855molecular_function3-dehydroquinate dehydratase activity
F0008652biological_processamino acid biosynthetic process
F0009073biological_processaromatic amino acid family biosynthetic process
F0009423biological_processchorismate biosynthetic process
F0016829molecular_functionlyase activity
G0003855molecular_function3-dehydroquinate dehydratase activity
G0008652biological_processamino acid biosynthetic process
G0009073biological_processaromatic amino acid family biosynthetic process
G0009423biological_processchorismate biosynthetic process
G0016829molecular_functionlyase activity
H0003855molecular_function3-dehydroquinate dehydratase activity
H0008652biological_processamino acid biosynthetic process
H0009073biological_processaromatic amino acid family biosynthetic process
H0009423biological_processchorismate biosynthetic process
H0016829molecular_functionlyase activity
I0003855molecular_function3-dehydroquinate dehydratase activity
I0008652biological_processamino acid biosynthetic process
I0009073biological_processaromatic amino acid family biosynthetic process
I0009423biological_processchorismate biosynthetic process
I0016829molecular_functionlyase activity
J0003855molecular_function3-dehydroquinate dehydratase activity
J0008652biological_processamino acid biosynthetic process
J0009073biological_processaromatic amino acid family biosynthetic process
J0009423biological_processchorismate biosynthetic process
J0016829molecular_functionlyase activity
K0003855molecular_function3-dehydroquinate dehydratase activity
K0008652biological_processamino acid biosynthetic process
K0009073biological_processaromatic amino acid family biosynthetic process
K0009423biological_processchorismate biosynthetic process
K0016829molecular_functionlyase activity
L0003855molecular_function3-dehydroquinate dehydratase activity
L0008652biological_processamino acid biosynthetic process
L0009073biological_processaromatic amino acid family biosynthetic process
L0009423biological_processchorismate biosynthetic process
L0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue TLA A 201
ChainResidue
AASN77
AALA79
AHIS83
AHIS103
ALEU104
ASER105
AARG110
AARG114
AHOH330

site_idAC2
Number of Residues10
Detailsbinding site for residue TLA B 201
ChainResidue
BASN77
BALA79
BALA80
BHIS83
BHIS103
BLEU104
BSER105
BARG114
BHOH315
BHOH319

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL B 202
ChainResidue
BASP40
BGLU41
BLEU44
BHOH308
BHOH333
KHIS0
KASN46

site_idAC4
Number of Residues9
Detailsbinding site for residue TLA C 201
ChainResidue
CASN77
CALA79
CALA80
CHIS83
CHIS103
CLEU104
CSER105
CARG114
CHOH320

site_idAC5
Number of Residues11
Detailsbinding site for residue TLA D 201
ChainResidue
DASN77
DALA79
DALA80
DTHR82
DHIS83
DHIS103
DLEU104
DSER105
DARG114
DHOH336
DHOH350

site_idAC6
Number of Residues10
Detailsbinding site for residue TLA E 201
ChainResidue
EASN77
EALA79
EALA80
EHIS83
EHIS103
ELEU104
ESER105
EARG110
EARG114
EHOH325

site_idAC7
Number of Residues10
Detailsbinding site for residue TLA F 201
ChainResidue
FASN77
FALA79
FALA80
FHIS83
FHIS103
FLEU104
FSER105
FVAL107
FARG114
FHOH312

site_idAC8
Number of Residues9
Detailsbinding site for residue TLA G 201
ChainResidue
GASN77
GALA79
GALA80
GHIS83
GHIS103
GLEU104
GSER105
GVAL107
GARG114

site_idAC9
Number of Residues9
Detailsbinding site for residue TLA H 201
ChainResidue
HASN77
HALA79
HALA80
HHIS83
HHIS103
HLEU104
HSER105
HARG114
HHOH336

site_idAD1
Number of Residues10
Detailsbinding site for residue TLA I 201
ChainResidue
IASN77
IALA79
IALA80
IHIS83
IHIS103
ILEU104
ISER105
IVAL107
IARG114
IHOH319

site_idAD2
Number of Residues11
Detailsbinding site for residue TLA J 201
ChainResidue
JHIS103
JLEU104
JSER105
JARG114
JHOH330
JHOH337
JASN77
JALA79
JALA80
JTHR82
JHIS83

site_idAD3
Number of Residues9
Detailsbinding site for residue TLA K 201
ChainResidue
KASN77
KALA79
KALA80
KHIS83
KHIS103
KLEU104
KSER105
KVAL107
KARG114

site_idAD4
Number of Residues4
Detailsbinding site for residue MPO K 202
ChainResidue
KGLN3
KGLU69
KLYS70
KASP72

site_idAD5
Number of Residues10
Detailsbinding site for residue TLA L 201
ChainResidue
LASN77
LALA79
LALA80
LHIS83
LHIS103
LLEU104
LSER105
LVAL107
LARG114
LHOH340

Functional Information from PROSITE/UniProt
site_idPS01029
Number of Residues18
DetailsDEHYDROQUINASE_II Dehydroquinase class II signature. LNGPNLnlLGqREpevYG
ChainResidueDetails
ALEU10-GLY27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00169
ChainResidueDetails
ATYR26
JTYR26
KTYR26
LTYR26
BTYR26
CTYR26
DTYR26
ETYR26
FTYR26
GTYR26
HTYR26
ITYR26

site_idSWS_FT_FI2
Number of Residues12
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00169
ChainResidueDetails
AHIS103
JHIS103
KHIS103
LHIS103
BHIS103
CHIS103
DHIS103
EHIS103
FHIS103
GHIS103
HHIS103
IHIS103

site_idSWS_FT_FI3
Number of Residues60
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00169
ChainResidueDetails
AASN77
BARG114
CASN77
CHIS83
CASP90
CLEU104
CARG114
DASN77
DHIS83
DASP90
DLEU104
AHIS83
DARG114
EASN77
EHIS83
EASP90
ELEU104
EARG114
FASN77
FHIS83
FASP90
FLEU104
AASP90
FARG114
GASN77
GHIS83
GASP90
GLEU104
GARG114
HASN77
HHIS83
HASP90
HLEU104
ALEU104
HARG114
IASN77
IHIS83
IASP90
ILEU104
IARG114
JASN77
JHIS83
JASP90
JLEU104
AARG114
JARG114
KASN77
KHIS83
KASP90
KLEU104
KARG114
LASN77
LHIS83
LASP90
LLEU104
BASN77
LARG114
BHIS83
BASP90
BLEU104

site_idSWS_FT_FI4
Number of Residues12
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00169
ChainResidueDetails
AARG21
JARG21
KARG21
LARG21
BARG21
CARG21
DARG21
EARG21
FARG21
GARG21
HARG21
IARG21

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PDB entries from 2024-07-10

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