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2C11

Crystal structure of the 2-hydrazinopyridine of semicarbazide- sensitive amine oxidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005769cellular_componentearly endosome
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0005902cellular_componentmicrovillus
A0006954biological_processinflammatory response
A0007155biological_processcell adhesion
A0008131molecular_functionprimary amine oxidase activity
A0009308biological_processamine metabolic process
A0009986cellular_componentcell surface
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
A0042802molecular_functionidentical protein binding
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
A0046982molecular_functionprotein heterodimerization activity
A0048038molecular_functionquinone binding
A0052595molecular_functionaliphatic amine oxidase activity
B0005507molecular_functioncopper ion binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005769cellular_componentearly endosome
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0005886cellular_componentplasma membrane
B0005902cellular_componentmicrovillus
B0006954biological_processinflammatory response
B0007155biological_processcell adhesion
B0008131molecular_functionprimary amine oxidase activity
B0009308biological_processamine metabolic process
B0009986cellular_componentcell surface
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
B0042802molecular_functionidentical protein binding
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
B0046982molecular_functionprotein heterodimerization activity
B0048038molecular_functionquinone binding
B0052595molecular_functionaliphatic amine oxidase activity
C0005507molecular_functioncopper ion binding
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005769cellular_componentearly endosome
C0005783cellular_componentendoplasmic reticulum
C0005794cellular_componentGolgi apparatus
C0005886cellular_componentplasma membrane
C0005902cellular_componentmicrovillus
C0006954biological_processinflammatory response
C0007155biological_processcell adhesion
C0008131molecular_functionprimary amine oxidase activity
C0009308biological_processamine metabolic process
C0009986cellular_componentcell surface
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
C0042802molecular_functionidentical protein binding
C0046677biological_processresponse to antibiotic
C0046872molecular_functionmetal ion binding
C0046982molecular_functionprotein heterodimerization activity
C0048038molecular_functionquinone binding
C0052595molecular_functionaliphatic amine oxidase activity
D0005507molecular_functioncopper ion binding
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005769cellular_componentearly endosome
D0005783cellular_componentendoplasmic reticulum
D0005794cellular_componentGolgi apparatus
D0005886cellular_componentplasma membrane
D0005902cellular_componentmicrovillus
D0006954biological_processinflammatory response
D0007155biological_processcell adhesion
D0008131molecular_functionprimary amine oxidase activity
D0009308biological_processamine metabolic process
D0009986cellular_componentcell surface
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
D0042802molecular_functionidentical protein binding
D0046677biological_processresponse to antibiotic
D0046872molecular_functionmetal ion binding
D0046982molecular_functionprotein heterodimerization activity
D0048038molecular_functionquinone binding
D0052595molecular_functionaliphatic amine oxidase activity
Functional Information from PROSITE/UniProt
site_idPS01164
Number of Residues14
DetailsCOPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVrsmsTllNYDY
ChainResidueDetails
ALEU460-TYR473

site_idPS01165
Number of Residues14
DetailsCOPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TaGflHIphaEDiP
ChainResidueDetails
ATHR679-PRO692

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P19801
ChainResidueDetails
AASP386
BASP386
CASP386
DASP386

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:16046623, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1
ChainResidueDetails
APAQ471
BPAQ471
CPAQ471
DPAQ471

site_idSWS_FT_FI3
Number of Residues52
DetailsBINDING: BINDING => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY
ChainResidueDetails
AHIS520
AGLU667
AASP673
ALEU674
AHIS684
BHIS520
BHIS522
BASP529
BLEU530
BASP531
BGLU572
AHIS522
BGLU641
BPHE663
BASN665
BGLU667
BASP673
BLEU674
BHIS684
CHIS520
CHIS522
CASP529
AASP529
CLEU530
CASP531
CGLU572
CGLU641
CPHE663
CASN665
CGLU667
CASP673
CLEU674
CHIS684
ALEU530
DHIS520
DHIS522
DASP529
DLEU530
DASP531
DGLU572
DGLU641
DPHE663
DASN665
DGLU667
AASP531
DASP673
DLEU674
DHIS684
AGLU572
AGLU641
APHE663
AASN665

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:16046623, ECO:0007744|PDB:1PU4
ChainResidueDetails
APAQ471
BPAQ471
CPAQ471
DPAQ471

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: O-linked (GalNAc...) serine => ECO:0000305|PubMed:16046623
ChainResidueDetails
ASER43
BSER43
CSER43
DSER43

site_idSWS_FT_FI6
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:19159218, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1
ChainResidueDetails
AASN137
BASN137
CASN137
DASN137

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: O-linked (GalNAc...) threonine => ECO:0000305|PubMed:16046623
ChainResidueDetails
ATHR212
BTHR212
CTHR212
DTHR212

site_idSWS_FT_FI8
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY
ChainResidueDetails
AASN232
BASN232
CASN232
DASN232

site_idSWS_FT_FI9
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTY
ChainResidueDetails
AASN294
BASN294
CASN294
DASN294

site_idSWS_FT_FI10
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY
ChainResidueDetails
AASN592
BASN592
CASN592
DASN592

site_idSWS_FT_FI11
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX
ChainResidueDetails
AASN618
BASN618
CASN618
DASN618

site_idSWS_FT_FI12
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY
ChainResidueDetails
AASN666
BASN666
CASN666
DASN666

site_idSWS_FT_FI13
Number of Residues4
DetailsCARBOHYD: O-linked (GlcNAc) threonine => ECO:0000305|PubMed:16046623
ChainResidueDetails
ATHR679
BTHR679
CTHR679
DTHR679

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
AASP386

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
BASP386

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
CASP386

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
DASP386

224004

PDB entries from 2024-08-21

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