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1FSJ

CRYSTAL STRUCTURE OF THE E9 DNASE DOMAIN

Functional Information from GO Data
ChainGOidnamespacecontents
B0004519molecular_functionendonuclease activity
B0005102molecular_functionsignaling receptor binding
B0009617biological_processresponse to bacterium
B0019835biological_processcytolysis
C0004519molecular_functionendonuclease activity
C0005102molecular_functionsignaling receptor binding
C0009617biological_processresponse to bacterium
C0019835biological_processcytolysis
D0004519molecular_functionendonuclease activity
D0005102molecular_functionsignaling receptor binding
D0009617biological_processresponse to bacterium
D0019835biological_processcytolysis
E0004519molecular_functionendonuclease activity
E0005102molecular_functionsignaling receptor binding
E0009617biological_processresponse to bacterium
E0019835biological_processcytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 B 801
ChainResidue
BARG5
BLEU101
BHIS102
BHIS103
BHIS127
BHIS131
BZN901
BHOH932
BHOH973

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 C 802
ChainResidue
CARG205
CHIS302
CHIS303
CHIS327
CZN902
CHOH908
CHOH937
ELYS734

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 D 803
ChainResidue
BLYS134
DHOH28
DHOH43
DHOH111
DARG405
DHIS502
DHIS503
DHIS527
DZN903

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 E 804
ChainResidue
EHOH31
EHOH298
EARG605
ELEU701
EHIS702
EHIS703
EHIS727
EHIS731
EZN904

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 901
ChainResidue
BHIS102
BHIS127
BHIS131
BPO4801
BHOH932

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 902
ChainResidue
CHIS302
CHIS327
CHIS331
CPO4802
CHOH911

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 903
ChainResidue
DHOH28
DHIS502
DHIS527
DHIS531
DPO4803

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN E 904
ChainResidue
EHOH31
EHIS702
EHIS727
EHIS731
EPO4804

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues128
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues44
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues52
DetailsCompositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 791
ChainResidueDetails

site_idMCSA2
Number of Residues7
DetailsM-CSA 791
ChainResidueDetails
BARG5electrostatic stabiliser
BARG96electrostatic stabiliser
BGLU100electrostatic stabiliser
BHIS102metal ligand
BHIS103increase nucleophilicity, proton acceptor, proton donor
BHIS127metal ligand
BHIS131metal ligand

site_idMCSA3
Number of Residues7
DetailsM-CSA 791
ChainResidueDetails
CARG205electrostatic stabiliser
CARG296electrostatic stabiliser
CGLU300electrostatic stabiliser
CHIS302metal ligand
CHIS303increase nucleophilicity, proton acceptor, proton donor
CHIS327metal ligand
CHIS331metal ligand

site_idMCSA4
Number of Residues7
DetailsM-CSA 791
ChainResidueDetails
DARG405electrostatic stabiliser
DARG496electrostatic stabiliser
DGLU500electrostatic stabiliser
DHIS502metal ligand
DHIS503increase nucleophilicity, proton acceptor, proton donor
DHIS527metal ligand
DHIS531metal ligand

246704

PDB entries from 2025-12-24

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