Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3W3D

Crystal structure of smooth muscle G actin DNase I complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0016787molecular_functionhydrolase activity
B0002283biological_processneutrophil activation involved in immune response
B0002673biological_processregulation of acute inflammatory response
B0003677molecular_functionDNA binding
B0003779molecular_functionactin binding
B0003824molecular_functioncatalytic activity
B0004519molecular_functionendonuclease activity
B0004530molecular_functiondeoxyribonuclease I activity
B0004536molecular_functionDNA nuclease activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005635cellular_componentnuclear envelope
B0006308biological_processDNA catabolic process
B0006915biological_processapoptotic process
B0031410cellular_componentcytoplasmic vesicle
B0042588cellular_componentzymogen granule
B0070948biological_processregulation of neutrophil mediated cytotoxicity
Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR52-GLY62

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WISKqEYDE
ChainResidueDetails
ATRP355-GLU363

site_idPS00918
Number of Residues8
DetailsDNASE_I_2 Deoxyribonuclease I signature 2. GDFNAdCS
ChainResidueDetails
BGLY167-SER174

site_idPS00919
Number of Residues21
DetailsDNASE_I_1 Deoxyribonuclease I signature 1. IVALHSAPsdavaEINsLyDV
ChainResidueDetails
BILE130-VAL150

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU103-ARG115

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2395459
ChainResidueDetails
BGLU78

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:4976790
ChainResidueDetails
BHIS134
AMET46

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Involved in actin-binding => ECO:0000269|PubMed:2395459
ChainResidueDetails
BGLU13
BVAL67

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme
ChainResidueDetails
BTYR65

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1748997, ECO:0000269|PubMed:3560229
ChainResidueDetails
BASN18

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 41
ChainResidueDetails
BGLU39metal ligand
BTYR76electrostatic stabiliser
BGLU78electrostatic stabiliser, increase acidity, increase basicity
BHIS134proton acceptor, proton donor
BASP168metal ligand
BASP212electrostatic stabiliser, increase acidity, increase basicity
BHIS252proton acceptor, proton donor

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon