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1FPY

CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM WITH INHIBITOR PHOSPHINOTHRICIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004356molecular_functionglutamine synthetase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006541biological_processglutamine metabolic process
A0006542biological_processglutamine biosynthetic process
A0016020cellular_componentmembrane
A0016874molecular_functionligase activity
A0019740biological_processnitrogen utilization
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
A0051260biological_processprotein homooligomerization
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004356molecular_functionglutamine synthetase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006541biological_processglutamine metabolic process
B0006542biological_processglutamine biosynthetic process
B0016020cellular_componentmembrane
B0016874molecular_functionligase activity
B0019740biological_processnitrogen utilization
B0030145molecular_functionmanganese ion binding
B0046872molecular_functionmetal ion binding
B0051260biological_processprotein homooligomerization
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0004356molecular_functionglutamine synthetase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006541biological_processglutamine metabolic process
C0006542biological_processglutamine biosynthetic process
C0016020cellular_componentmembrane
C0016874molecular_functionligase activity
C0019740biological_processnitrogen utilization
C0030145molecular_functionmanganese ion binding
C0046872molecular_functionmetal ion binding
C0051260biological_processprotein homooligomerization
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0004356molecular_functionglutamine synthetase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006541biological_processglutamine metabolic process
D0006542biological_processglutamine biosynthetic process
D0016020cellular_componentmembrane
D0016874molecular_functionligase activity
D0019740biological_processnitrogen utilization
D0030145molecular_functionmanganese ion binding
D0046872molecular_functionmetal ion binding
D0051260biological_processprotein homooligomerization
E0000166molecular_functionnucleotide binding
E0003824molecular_functioncatalytic activity
E0004356molecular_functionglutamine synthetase activity
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0006541biological_processglutamine metabolic process
E0006542biological_processglutamine biosynthetic process
E0016020cellular_componentmembrane
E0016874molecular_functionligase activity
E0019740biological_processnitrogen utilization
E0030145molecular_functionmanganese ion binding
E0046872molecular_functionmetal ion binding
E0051260biological_processprotein homooligomerization
F0000166molecular_functionnucleotide binding
F0003824molecular_functioncatalytic activity
F0004356molecular_functionglutamine synthetase activity
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0006541biological_processglutamine metabolic process
F0006542biological_processglutamine biosynthetic process
F0016020cellular_componentmembrane
F0016874molecular_functionligase activity
F0019740biological_processnitrogen utilization
F0030145molecular_functionmanganese ion binding
F0046872molecular_functionmetal ion binding
F0051260biological_processprotein homooligomerization
G0000166molecular_functionnucleotide binding
G0003824molecular_functioncatalytic activity
G0004356molecular_functionglutamine synthetase activity
G0005524molecular_functionATP binding
G0005737cellular_componentcytoplasm
G0006541biological_processglutamine metabolic process
G0006542biological_processglutamine biosynthetic process
G0016020cellular_componentmembrane
G0016874molecular_functionligase activity
G0019740biological_processnitrogen utilization
G0030145molecular_functionmanganese ion binding
G0046872molecular_functionmetal ion binding
G0051260biological_processprotein homooligomerization
H0000166molecular_functionnucleotide binding
H0003824molecular_functioncatalytic activity
H0004356molecular_functionglutamine synthetase activity
H0005524molecular_functionATP binding
H0005737cellular_componentcytoplasm
H0006541biological_processglutamine metabolic process
H0006542biological_processglutamine biosynthetic process
H0016020cellular_componentmembrane
H0016874molecular_functionligase activity
H0019740biological_processnitrogen utilization
H0030145molecular_functionmanganese ion binding
H0046872molecular_functionmetal ion binding
H0051260biological_processprotein homooligomerization
I0000166molecular_functionnucleotide binding
I0003824molecular_functioncatalytic activity
I0004356molecular_functionglutamine synthetase activity
I0005524molecular_functionATP binding
I0005737cellular_componentcytoplasm
I0006541biological_processglutamine metabolic process
I0006542biological_processglutamine biosynthetic process
I0016020cellular_componentmembrane
I0016874molecular_functionligase activity
I0019740biological_processnitrogen utilization
I0030145molecular_functionmanganese ion binding
I0046872molecular_functionmetal ion binding
I0051260biological_processprotein homooligomerization
J0000166molecular_functionnucleotide binding
J0003824molecular_functioncatalytic activity
J0004356molecular_functionglutamine synthetase activity
J0005524molecular_functionATP binding
J0005737cellular_componentcytoplasm
J0006541biological_processglutamine metabolic process
J0006542biological_processglutamine biosynthetic process
J0016020cellular_componentmembrane
J0016874molecular_functionligase activity
J0019740biological_processnitrogen utilization
J0030145molecular_functionmanganese ion binding
J0046872molecular_functionmetal ion binding
J0051260biological_processprotein homooligomerization
K0000166molecular_functionnucleotide binding
K0003824molecular_functioncatalytic activity
K0004356molecular_functionglutamine synthetase activity
K0005524molecular_functionATP binding
K0005737cellular_componentcytoplasm
K0006541biological_processglutamine metabolic process
K0006542biological_processglutamine biosynthetic process
K0016020cellular_componentmembrane
K0016874molecular_functionligase activity
K0019740biological_processnitrogen utilization
K0030145molecular_functionmanganese ion binding
K0046872molecular_functionmetal ion binding
K0051260biological_processprotein homooligomerization
L0000166molecular_functionnucleotide binding
L0003824molecular_functioncatalytic activity
L0004356molecular_functionglutamine synthetase activity
L0005524molecular_functionATP binding
L0005737cellular_componentcytoplasm
L0006541biological_processglutamine metabolic process
L0006542biological_processglutamine biosynthetic process
L0016020cellular_componentmembrane
L0016874molecular_functionligase activity
L0019740biological_processnitrogen utilization
L0030145molecular_functionmanganese ion binding
L0046872molecular_functionmetal ion binding
L0051260biological_processprotein homooligomerization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 469
ChainResidue
AGLU131
AGLU212
AGLU220
APPQ5900

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 470
ChainResidue
AGLU129
AHIS269
AGLU357
AADP4471
APPQ5900

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN B 469
ChainResidue
BGLU131
BGLU212
BGLU220
BPPQ5901

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 470
ChainResidue
BGLU129
BHIS269
BGLU357
BADP4472
BPPQ5901

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN C 469
ChainResidue
CGLU131
CGLU212
CGLU220
CPPQ5902

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN C 470
ChainResidue
CGLU129
CHIS269
CGLU357
CADP4473
CPPQ5902

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN D 469
ChainResidue
DGLU131
DGLU212
DGLU220
DPPQ5903

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN D 470
ChainResidue
DGLU129
DHIS269
DGLU357
DADP4474
DPPQ5903

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN E 469
ChainResidue
EGLU131
EGLU212
EGLU220
EPPQ5904

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN E 470
ChainResidue
EGLU129
EHIS269
EGLU357
EADP4475
EPPQ5904

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN F 469
ChainResidue
FGLU131
FGLU212
FGLU220
FPPQ5905

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN F 470
ChainResidue
FGLU129
FHIS269
FGLU357
FADP4476
FPPQ5905

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN G 469
ChainResidue
GGLU131
GGLU212
GGLU220
GPPQ5906

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN G 470
ChainResidue
GGLU129
GHIS269
GGLU357
GADP4477
GPPQ5906

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN H 469
ChainResidue
HGLU131
HGLU212
HGLU220
HPPQ5907

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN H 470
ChainResidue
HGLU129
HHIS269
HGLU357
HADP4478
HPPQ5907

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN I 469
ChainResidue
IGLU131
IGLU212
IGLU220
IPPQ5908

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN I 470
ChainResidue
IGLU129
IHIS269
IGLU357
IADP4479
IPPQ5908

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN J 469
ChainResidue
JGLU131
JGLU212
JGLU220
JPPQ5909

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN J 470
ChainResidue
JGLU129
JHIS269
JGLU357
JADP4480
JPPQ5909

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN K 469
ChainResidue
KGLU131
KGLU212
KGLU220
KPPQ5910

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN K 470
ChainResidue
KGLU129
KHIS269
KGLU357
KADP4481
KPPQ5910

site_idCC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN L 469
ChainResidue
LGLU131
LGLU212
LGLU220
LPPQ5911

site_idCC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN L 470
ChainResidue
LGLU129
LHIS269
LGLU357
LADP4482
LPPQ5911

site_idCC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP A 4471
ChainResidue
AGLY127
AGLU129
AGLU207
ATHR223
AARG224
APHE225
AHIS271
ASER273
AARG355
AGLU357
AMN470
AHOH5976
AHOH6045

site_idCC8
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP B 4472
ChainResidue
BGLY127
BGLU129
BGLU207
BTHR223
BARG224
BPHE225
BHIS271
BSER273
BARG355
BGLU357
BMN470
BHOH5977
BHOH6049

site_idCC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP C 4473
ChainResidue
CGLY127
CGLU129
CGLU207
CTHR223
CARG224
CPHE225
CHIS271
CSER273
CARG355
CGLU357
CMN470
CHOH5976
CHOH6046

site_idDC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP D 4474
ChainResidue
DGLY127
DGLU129
DGLU207
DTHR223
DARG224
DPHE225
DHIS271
DSER273
DARG355
DGLU357
DMN470
DHOH5979
DHOH6049

site_idDC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP E 4475
ChainResidue
EGLY127
EGLU129
EGLU207
ETHR223
EARG224
EPHE225
EHIS271
ESER273
EARG355
EGLU357
EMN470
EHOH691
EHOH849

site_idDC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP F 4476
ChainResidue
FGLY127
FGLU129
FGLU207
FTHR223
FARG224
FPHE225
FHIS271
FSER273
FARG355
FGLU357
FMN470
FHOH5908
FHOH5986

site_idDC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP G 4477
ChainResidue
GGLY127
GGLU129
GGLU207
GTHR223
GARG224
GPHE225
GHIS271
GSER273
GARG355
GGLU357
GMN470
GHOH5986
GHOH6058

site_idDC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP H 4478
ChainResidue
HGLY127
HGLU129
HGLU207
HTHR223
HARG224
HPHE225
HHIS271
HSER273
HARG355
HGLU357
HMN470
HHOH5914
HHOH5990

site_idDC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP I 4479
ChainResidue
IGLY127
IGLU129
IGLU207
ITHR223
IARG224
IPHE225
IHIS271
ISER273
IARG355
IGLU357
IMN470
IHOH5918
IHOH5997

site_idDC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP J 4480
ChainResidue
JGLY127
JGLU129
JGLU207
JTHR223
JARG224
JPHE225
JHIS271
JSER273
JARG355
JGLU357
JMN470
JHOH5916
JHOH5993

site_idDC8
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP K 4481
ChainResidue
KGLY127
KGLU129
KGLU207
KTHR223
KARG224
KPHE225
KHIS271
KSER273
KARG355
KGLU357
KMN470
KHOH1461
KHOH1609

site_idDC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP L 4482
ChainResidue
LGLY127
LGLU129
LGLU207
LTHR223
LARG224
LPHE225
LHIS271
LSER273
LARG355
LGLU357
LMN470
LHOH1614
LHOH1762

site_idEC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PPQ A 5900
ChainResidue
AGLU131
AGLU212
AASN264
AGLY265
ASER266
AGLY267
AHIS269
AARG321
AGLU327
AARG359
AMN469
AMN470

site_idEC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PPQ B 5901
ChainResidue
BGLU131
BGLU212
BASN264
BGLY265
BSER266
BGLY267
BHIS269
BARG321
BGLU327
BARG359
BMN469
BMN470

site_idEC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PPQ C 5902
ChainResidue
CGLU131
CGLU212
CASN264
CGLY265
CSER266
CGLY267
CHIS269
CARG321
CGLU327
CARG359
CMN469
CMN470

site_idEC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PPQ D 5903
ChainResidue
DGLU131
DGLU212
DASN264
DGLY265
DSER266
DGLY267
DHIS269
DARG321
DGLU327
DARG359
DMN469
DMN470

site_idEC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PPQ E 5904
ChainResidue
EGLU131
EGLU212
EASN264
EGLY265
ESER266
EGLY267
EHIS269
EARG321
EGLU327
EARG359
EMN469
EMN470

site_idEC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PPQ F 5905
ChainResidue
FGLU131
FGLU212
FASN264
FGLY265
FSER266
FGLY267
FHIS269
FARG321
FGLU327
FARG359
FMN469
FMN470

site_idEC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PPQ G 5906
ChainResidue
GGLU131
GGLU212
GASN264
GGLY265
GSER266
GGLY267
GHIS269
GARG321
GGLU327
GARG359
GMN469
GMN470

site_idEC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PPQ H 5907
ChainResidue
HGLU131
HGLU212
HASN264
HGLY265
HSER266
HGLY267
HHIS269
HARG321
HGLU327
HARG359
HMN469
HMN470

site_idEC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PPQ I 5908
ChainResidue
IGLU131
IGLU212
IASN264
IGLY265
ISER266
IGLY267
IHIS269
IARG321
IGLU327
IARG359
IMN469
IMN470

site_idFC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PPQ J 5909
ChainResidue
JGLU131
JGLU212
JASN264
JGLY265
JSER266
JGLY267
JHIS269
JARG321
JGLU327
JARG359
JMN469
JMN470

site_idFC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PPQ K 5910
ChainResidue
KGLU131
KGLU212
KASN264
KGLY265
KSER266
KGLY267
KHIS269
KARG321
KGLU327
KARG359
KMN469
KMN470

site_idFC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PPQ L 5911
ChainResidue
LGLU131
LGLU212
LASN264
LGLY265
LSER266
LGLY267
LHIS269
LARG321
LGLU327
LARG359
LMN469
LMN470

Functional Information from PROSITE/UniProt
site_idPS00180
Number of Residues19
DetailsGLNA_1 Glutamine synthetase signature 1. FDGSSiggwkginESDmvL
ChainResidueDetails
APHE49-LEU67

site_idPS00181
Number of Residues16
DetailsGLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPMfgd..NGSGmHchmS
ChainResidueDetails
ALYS258-SER273

site_idPS00182
Number of Residues13
DetailsGLNA_ADENYLATION Glutamine synthetase class-I adenylation site. KIhpgepMDKNLY
ChainResidueDetails
ALYS385-TYR397

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1008
DetailsDomain: {"description":"GS beta-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU01330","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4368
DetailsDomain: {"description":"GS catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU01331","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2572586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8099447","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GLS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LGS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7727369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8099447","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LGR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LGS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7727369","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LGR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7727369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8099447","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1F1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LGR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LGS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P12425","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P77961","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8099447","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LGS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P9WN39","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2572586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7727369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8099447","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LGR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GLS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LGS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8099447","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2LGS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues12
DetailsModified residue: {"description":"O-AMP-tyrosine","evidences":[{"source":"UniProtKB","id":"P9WN39","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hto
ChainResidueDetails
AARG339
AASP50
AGLU327

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hto
ChainResidueDetails
JARG339
JASP50
JGLU327

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hto
ChainResidueDetails
KARG339
KASP50
KGLU327

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hto
ChainResidueDetails
LARG339
LASP50
LGLU327

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hto
ChainResidueDetails
BARG339
BASP50
BGLU327

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hto
ChainResidueDetails
CARG339
CASP50
CGLU327

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hto
ChainResidueDetails
DARG339
DASP50
DGLU327

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hto
ChainResidueDetails
EARG339
EASP50
EGLU327

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hto
ChainResidueDetails
FARG339
FASP50
FGLU327

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hto
ChainResidueDetails
GARG339
GASP50
GGLU327

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hto
ChainResidueDetails
HARG339
HASP50
HGLU327

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hto
ChainResidueDetails
IARG339
IASP50
IGLU327

239492

PDB entries from 2025-07-30

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