3W3D
Crystal structure of smooth muscle G actin DNase I complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0015629 | cellular_component | actin cytoskeleton |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0071944 | cellular_component | cell periphery |
| B | 0002283 | biological_process | neutrophil activation involved in immune response |
| B | 0002673 | biological_process | regulation of acute inflammatory response |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003779 | molecular_function | actin binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0004530 | molecular_function | deoxyribonuclease I activity |
| B | 0004536 | molecular_function | DNA nuclease activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005634 | cellular_component | nucleus |
| B | 0005635 | cellular_component | nuclear envelope |
| B | 0006308 | biological_process | DNA catabolic process |
| B | 0006915 | biological_process | apoptotic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0031410 | cellular_component | cytoplasmic vesicle |
| B | 0042588 | cellular_component | zymogen granule |
| B | 0070948 | biological_process | regulation of neutrophil mediated cytotoxicity |
Functional Information from PROSITE/UniProt
| site_id | PS00406 |
| Number of Residues | 11 |
| Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
| Chain | Residue | Details |
| A | TYR52-GLY62 |
| site_id | PS00432 |
| Number of Residues | 9 |
| Details | ACTINS_2 Actins signature 2. WISKqEYDE |
| Chain | Residue | Details |
| A | TRP355-GLU363 |
| site_id | PS00918 |
| Number of Residues | 8 |
| Details | DNASE_I_2 Deoxyribonuclease I signature 2. GDFNAdCS |
| Chain | Residue | Details |
| B | GLY167-SER174 |
| site_id | PS00919 |
| Number of Residues | 21 |
| Details | DNASE_I_1 Deoxyribonuclease I signature 1. IVALHSAPsdavaEINsLyDV |
| Chain | Residue | Details |
| B | ILE130-VAL150 |
| site_id | PS01132 |
| Number of Residues | 13 |
| Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
| Chain | Residue | Details |
| A | LEU103-ARG115 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylglutamate; in Actin, gamma-enteric smooth muscle","evidences":[{"source":"UniProtKB","id":"P63267","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P63268","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1993","firstPage":"C111","lastPage":"C112","volume":"49","journal":"Acta Crystallogr. A","title":"Refined structure and solvent network of chicken gizzard G-actin DNase 1 complex at 1.8A resolution.","authors":["Sasaki K.","Sakabe K.","Sakabe N.","Kondo H.","Shimomur M."],"citationCrossReferences":[{"database":"DOI","id":"10.1107/S0108767378096798"}]}},{"source":"PDB","id":"3W3D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4976790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Involved in actin-binding","evidences":[{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Site: {"description":"Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1748997","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3560229","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 41 |
| Chain | Residue | Details |
| B | GLU39 | metal ligand |
| B | TYR76 | electrostatic stabiliser |
| B | GLU78 | electrostatic stabiliser, increase acidity, increase basicity |
| B | HIS134 | proton acceptor, proton donor |
| B | ASP168 | metal ligand |
| B | ASP212 | electrostatic stabiliser, increase acidity, increase basicity |
| B | HIS252 | proton acceptor, proton donor |
