9FJY
Structure of the DNase I- and phalloidin-bound pointed end of F-actin (conformer 2).
Functional Information from PROSITE/UniProt
| site_id | PS00406 |
| Number of Residues | 11 |
| Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
| Chain | Residue | Details |
| A | TYR53-GLY63 |
| site_id | PS00432 |
| Number of Residues | 9 |
| Details | ACTINS_2 Actins signature 2. WISKqEYDE |
| Chain | Residue | Details |
| A | TRP356-GLU364 |
| site_id | PS00918 |
| Number of Residues | 8 |
| Details | DNASE_I_2 Deoxyribonuclease I signature 2. GDFNAdCS |
| Chain | Residue | Details |
| E | GLY167-SER174 |
| site_id | PS00919 |
| Number of Residues | 21 |
| Details | DNASE_I_1 Deoxyribonuclease I signature 1. IVALHSAPsdavaEINsLyDV |
| Chain | Residue | Details |
| E | ILE130-VAL150 |
| site_id | PS01132 |
| Number of Residues | 13 |
| Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
| Chain | Residue | Details |
| A | LEU104-ARG116 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:2395459 |
| Chain | Residue | Details |
| E | GLU78 | |
| F | GLU78 | |
| C | ASP2 | |
| D | ASP2 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:4976790 |
| Chain | Residue | Details |
| E | HIS134 | |
| F | HIS134 | |
| B | MET44 | |
| B | MET47 | |
| C | MET44 | |
| C | MET47 | |
| D | MET44 | |
| D | MET47 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Involved in actin-binding => ECO:0000269|PubMed:2395459 |
| Chain | Residue | Details |
| E | GLU13 | |
| E | VAL67 | |
| F | GLU13 | |
| F | VAL67 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme |
| Chain | Residue | Details |
| E | TYR65 | |
| F | TYR65 | |
| C | LYS84 | |
| D | LYS84 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1748997, ECO:0000269|PubMed:3560229 |
| Chain | Residue | Details |
| E | ASN18 | |
| F | ASN18 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 41 |
| Chain | Residue | Details |
| E | GLU39 | metal ligand |
| E | TYR76 | electrostatic stabiliser |
| E | GLU78 | electrostatic stabiliser, increase acidity, increase basicity |
| E | HIS134 | proton acceptor, proton donor |
| E | ASP168 | metal ligand |
| E | ASP212 | electrostatic stabiliser, increase acidity, increase basicity |
| E | HIS252 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 41 |
| Chain | Residue | Details |
| F | GLU39 | metal ligand |
| F | TYR76 | electrostatic stabiliser |
| F | GLU78 | electrostatic stabiliser, increase acidity, increase basicity |
| F | HIS134 | proton acceptor, proton donor |
| F | ASP168 | metal ligand |
| F | ASP212 | electrostatic stabiliser, increase acidity, increase basicity |
| F | HIS252 | proton acceptor, proton donor |
