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2DNJ

DNASE I-INDUCED DNA CONFORMATION. 2 ANGSTROMS STRUCTURE OF A DNASE I-OCTAMER COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0002283biological_processneutrophil activation involved in immune response
A0002673biological_processregulation of acute inflammatory response
A0003677molecular_functionDNA binding
A0003779molecular_functionactin binding
A0003824molecular_functioncatalytic activity
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004530molecular_functiondeoxyribonuclease I activity
A0004536molecular_functionDNA nuclease activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0006308biological_processDNA catabolic process
A0006915biological_processapoptotic process
A0016787molecular_functionhydrolase activity
A0031410cellular_componentcytoplasmic vesicle
A0042588cellular_componentzymogen granule
A0070948biological_processregulation of neutrophil mediated cytotoxicity
Functional Information from PDB Data
site_idACT
Number of Residues5
Details
ChainResidue
AGLU39
AGLU78
AHIS134
AASP212
AHIS252

Functional Information from PROSITE/UniProt
site_idPS00918
Number of Residues8
DetailsDNASE_I_2 Deoxyribonuclease I signature 2. GDFNAdCS
ChainResidueDetails
AGLY167-SER174

site_idPS00919
Number of Residues21
DetailsDNASE_I_1 Deoxyribonuclease I signature 1. IVALHSAPsdavaEINsLyDV
ChainResidueDetails
AILE130-VAL150

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4976790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Involved in actin-binding","evidences":[{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1748997","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3560229","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dnk
ChainResidueDetails
AASP212
AHIS134
AGLU78
AHIS252

site_idMCSA1
Number of Residues7
DetailsM-CSA 41
ChainResidueDetails

246031

PDB entries from 2025-12-10

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