4FDG
Crystal Structure of an Archaeal MCM Filament
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003697 | molecular_function | single-stranded DNA binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0017116 | molecular_function | single-stranded DNA helicase activity |
| A | 0042555 | cellular_component | MCM complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043138 | molecular_function | 3'-5' DNA helicase activity |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003697 | molecular_function | single-stranded DNA binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0017116 | molecular_function | single-stranded DNA helicase activity |
| B | 0042555 | cellular_component | MCM complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043138 | molecular_function | 3'-5' DNA helicase activity |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003697 | molecular_function | single-stranded DNA binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0017116 | molecular_function | single-stranded DNA helicase activity |
| C | 0042555 | cellular_component | MCM complex |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0043138 | molecular_function | 3'-5' DNA helicase activity |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003697 | molecular_function | single-stranded DNA binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0017116 | molecular_function | single-stranded DNA helicase activity |
| D | 0042555 | cellular_component | MCM complex |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0043138 | molecular_function | 3'-5' DNA helicase activity |
| E | 0003677 | molecular_function | DNA binding |
| E | 0003697 | molecular_function | single-stranded DNA binding |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0017116 | molecular_function | single-stranded DNA helicase activity |
| E | 0042555 | cellular_component | MCM complex |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0043138 | molecular_function | 3'-5' DNA helicase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 701 |
| Chain | Residue |
| B | HIS144 |
| B | CYS149 |
| B | CYS171 |
| B | CYS174 |
| B | LYS176 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 701 |
| Chain | Residue |
| A | HIS144 |
| A | CYS149 |
| A | CYS171 |
| A | CYS174 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 701 |
| Chain | Residue |
| C | HIS144 |
| C | CYS149 |
| C | CYS171 |
| C | CYS174 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 701 |
| Chain | Residue |
| D | HIS144 |
| D | CYS149 |
| D | CYS171 |
| D | CYS174 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 701 |
| Chain | Residue |
| E | HIS144 |
| E | CYS149 |
| E | CYS171 |
| E | CYS174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 35 |
| Details | Motif: {"description":"Walker A","evidences":[{"source":"PROSITE-ProRule","id":"PRU01410","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | Motif: {"description":"Walker B","evidences":[{"source":"PROSITE-ProRule","id":"PRU01410","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18417534","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36499022","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VL6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FDG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6MII","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 50 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"36499022","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31308367","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6MII","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 25 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31308367","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36499022","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6MII","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31308367","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6MII","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 5 |
| Details | Site: {"description":"Arginine finger","evidences":[{"source":"PROSITE-ProRule","id":"PRU01410","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17964268","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |






