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1F8S

CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.

Functional Information from GO Data
ChainGOidnamespacecontents
A0001716molecular_functionL-amino-acid oxidase activity
A0005576cellular_componentextracellular region
A0006915biological_processapoptotic process
A0009063biological_processamino acid catabolic process
A0016491molecular_functionoxidoreductase activity
A0031640biological_processkilling of cells of another organism
A0035821biological_processmodulation of process of another organism
A0042742biological_processdefense response to bacterium
A0090729molecular_functiontoxin activity
A0106329molecular_functionL-phenylalaine oxidase activity
B0001716molecular_functionL-amino-acid oxidase activity
B0005576cellular_componentextracellular region
B0006915biological_processapoptotic process
B0009063biological_processamino acid catabolic process
B0016491molecular_functionoxidoreductase activity
B0031640biological_processkilling of cells of another organism
B0035821biological_processmodulation of process of another organism
B0042742biological_processdefense response to bacterium
B0090729molecular_functiontoxin activity
B0106329molecular_functionL-phenylalaine oxidase activity
C0001716molecular_functionL-amino-acid oxidase activity
C0005576cellular_componentextracellular region
C0006915biological_processapoptotic process
C0009063biological_processamino acid catabolic process
C0016491molecular_functionoxidoreductase activity
C0031640biological_processkilling of cells of another organism
C0035821biological_processmodulation of process of another organism
C0042742biological_processdefense response to bacterium
C0090729molecular_functiontoxin activity
C0106329molecular_functionL-phenylalaine oxidase activity
D0001716molecular_functionL-amino-acid oxidase activity
D0005576cellular_componentextracellular region
D0006915biological_processapoptotic process
D0009063biological_processamino acid catabolic process
D0016491molecular_functionoxidoreductase activity
D0031640biological_processkilling of cells of another organism
D0035821biological_processmodulation of process of another organism
D0042742biological_processdefense response to bacterium
D0090729molecular_functiontoxin activity
D0106329molecular_functionL-phenylalaine oxidase activity
E0001716molecular_functionL-amino-acid oxidase activity
E0005576cellular_componentextracellular region
E0006915biological_processapoptotic process
E0009063biological_processamino acid catabolic process
E0016491molecular_functionoxidoreductase activity
E0031640biological_processkilling of cells of another organism
E0035821biological_processmodulation of process of another organism
E0042742biological_processdefense response to bacterium
E0090729molecular_functiontoxin activity
E0106329molecular_functionL-phenylalaine oxidase activity
F0001716molecular_functionL-amino-acid oxidase activity
F0005576cellular_componentextracellular region
F0006915biological_processapoptotic process
F0009063biological_processamino acid catabolic process
F0016491molecular_functionoxidoreductase activity
F0031640biological_processkilling of cells of another organism
F0035821biological_processmodulation of process of another organism
F0042742biological_processdefense response to bacterium
F0090729molecular_functiontoxin activity
F0106329molecular_functionL-phenylalaine oxidase activity
G0001716molecular_functionL-amino-acid oxidase activity
G0005576cellular_componentextracellular region
G0006915biological_processapoptotic process
G0009063biological_processamino acid catabolic process
G0016491molecular_functionoxidoreductase activity
G0031640biological_processkilling of cells of another organism
G0035821biological_processmodulation of process of another organism
G0042742biological_processdefense response to bacterium
G0090729molecular_functiontoxin activity
G0106329molecular_functionL-phenylalaine oxidase activity
H0001716molecular_functionL-amino-acid oxidase activity
H0005576cellular_componentextracellular region
H0006915biological_processapoptotic process
H0009063biological_processamino acid catabolic process
H0016491molecular_functionoxidoreductase activity
H0031640biological_processkilling of cells of another organism
H0035821biological_processmodulation of process of another organism
H0042742biological_processdefense response to bacterium
H0090729molecular_functiontoxin activity
H0106329molecular_functionL-phenylalaine oxidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsBINDING: BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
ChainResidueDetails
AMET43
BGLY87
BVAL261
BGLU457
CMET43
CGLU63
CARG71
CGLY87
CVAL261
CGLU457
DMET43
AGLU63
DGLU63
DARG71
DGLY87
DVAL261
DGLU457
EMET43
EGLU63
EARG71
EGLY87
EVAL261
AARG71
EGLU457
FMET43
FGLU63
FARG71
FGLY87
FVAL261
FGLU457
GMET43
GGLU63
GARG71
AGLY87
GGLY87
GVAL261
GGLU457
HMET43
HGLU63
HARG71
HGLY87
HVAL261
HGLU457
AVAL261
AGLU457
BMET43
BGLU63
BARG71

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
ChainResidueDetails
AARG90
DARG90
DHIS223
DTYR372
EARG90
EHIS223
ETYR372
FARG90
FHIS223
FTYR372
GARG90
AHIS223
GHIS223
GTYR372
HARG90
HHIS223
HTYR372
ATYR372
BARG90
BHIS223
BTYR372
CARG90
CHIS223
CTYR372

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
ChainResidueDetails
AGLY464
BGLY464
CGLY464
DGLY464
EGLY464
FGLY464
GGLY464
HGLY464

site_idSWS_FT_FI4
Number of Residues16
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
ChainResidueDetails
AASN172
EASN361
FASN172
FASN361
GASN172
GASN361
HASN172
HASN361
AASN361
BASN172
BASN361
CASN172
CASN361
DASN172
DASN361
EASN172

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
ALYS326
AHIS223

site_idCSA10
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
BPRO92

site_idCSA11
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
CPRO92

site_idCSA12
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
DPRO92

site_idCSA13
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
EPRO92

site_idCSA14
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
FPRO92

site_idCSA15
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
GPRO92

site_idCSA16
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
HPRO92

site_idCSA17
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
AALA84

site_idCSA18
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
BALA84

site_idCSA19
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
CALA84

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
BLYS326
BHIS223

site_idCSA20
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
DALA84

site_idCSA21
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
EALA84

site_idCSA22
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
FALA84

site_idCSA23
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
GALA84

site_idCSA24
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
HALA84

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
CLYS326
CHIS223

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
DLYS326
DHIS223

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
ELYS326
EHIS223

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
FLYS326
FHIS223

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
GLYS326
GHIS223

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
HLYS326
HHIS223

site_idCSA9
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
APRO92

site_idMCSA1
Number of Residues2
DetailsM-CSA 555
ChainResidueDetails
AHIS223proton acceptor, proton donor
ALYS326proton acceptor

site_idMCSA2
Number of Residues2
DetailsM-CSA 555
ChainResidueDetails
BHIS223proton acceptor, proton donor
BLYS326proton acceptor

site_idMCSA3
Number of Residues2
DetailsM-CSA 555
ChainResidueDetails
CHIS223proton acceptor, proton donor
CLYS326proton acceptor

site_idMCSA4
Number of Residues2
DetailsM-CSA 555
ChainResidueDetails
DHIS223proton acceptor, proton donor
DLYS326proton acceptor

site_idMCSA5
Number of Residues2
DetailsM-CSA 555
ChainResidueDetails
EHIS223proton acceptor, proton donor
ELYS326proton acceptor

site_idMCSA6
Number of Residues2
DetailsM-CSA 555
ChainResidueDetails
FHIS223proton acceptor, proton donor
FLYS326proton acceptor

site_idMCSA7
Number of Residues2
DetailsM-CSA 555
ChainResidueDetails
GHIS223proton acceptor, proton donor
GLYS326proton acceptor

site_idMCSA8
Number of Residues2
DetailsM-CSA 555
ChainResidueDetails
HHIS223proton acceptor, proton donor
HLYS326proton acceptor

227111

PDB entries from 2024-11-06

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