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1DNK

THE X-RAY STRUCTURE OF THE DNASE I-D(GGTATACC)2 COMPLEX AT 2.3 ANGSTROMS RESOLUTION

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
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
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
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2395459
ChainResidueDetails
AGLU78

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:4976790
ChainResidueDetails
AHIS134

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Involved in actin-binding => ECO:0000269|PubMed:2395459
ChainResidueDetails
AGLU13
AVAL67

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme
ChainResidueDetails
ATYR65

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1748997, ECO:0000269|PubMed:3560229
ChainResidueDetails
AASN18

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 9000637
ChainResidueDetails
AASP212
AHIS134
AGLU78
AHIS252

site_idMCSA1
Number of Residues7
DetailsM-CSA 41
ChainResidueDetails
AGLU39metal ligand
ATYR76electrostatic stabiliser
AGLU78electrostatic stabiliser, increase acidity, increase basicity
AHIS134proton acceptor, proton donor
AASP168metal ligand
AASP212electrostatic stabiliser, increase acidity, increase basicity
AHIS252proton acceptor, proton donor

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PDB entries from 2024-10-30

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