4Q0Z
The catalytic core of Rad2 in complex with DNA substrate (complex III)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003697 | molecular_function | single-stranded DNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0006289 | biological_process | nucleotide-excision repair |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003697 | molecular_function | single-stranded DNA binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0006289 | biological_process | nucleotide-excision repair |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| E | 0003677 | molecular_function | DNA binding |
| E | 0003697 | molecular_function | single-stranded DNA binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004518 | molecular_function | nuclease activity |
| E | 0004519 | molecular_function | endonuclease activity |
| E | 0005634 | cellular_component | nucleus |
| E | 0006289 | biological_process | nucleotide-excision repair |
| E | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| F | 0003677 | molecular_function | DNA binding |
| F | 0003697 | molecular_function | single-stranded DNA binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004518 | molecular_function | nuclease activity |
| F | 0004519 | molecular_function | endonuclease activity |
| F | 0005634 | cellular_component | nucleus |
| F | 0006289 | biological_process | nucleotide-excision repair |
| F | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 1001 |
| Chain | Residue |
| A | GLU794 |
| A | ASP813 |
| A | ASP815 |
| A | HOH1117 |
| A | HOH1178 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K A 1002 |
| Chain | Residue |
| C | DG9 |
| D | DA9 |
| D | HOH116 |
| A | LEU869 |
| A | MET872 |
| A | HOH1126 |
| A | HOH1285 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 1001 |
| Chain | Residue |
| B | LYS84 |
| B | GLU794 |
| B | ASP813 |
| B | ASP815 |
| B | ASP864 |
| B | HOH1183 |
| B | HOH1224 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE K B 1002 |
| Chain | Residue |
| B | LEU860 |
| B | LEU861 |
| B | LEU869 |
| B | MET872 |
| B | HOH1135 |
| B | HOH1230 |
| C | DG9 |
| C | HOH102 |
| D | DA9 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA E 1001 |
| Chain | Residue |
| E | GLU794 |
| E | ASP813 |
| E | ASP815 |
| E | ASP864 |
| E | HOH1149 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K E 1002 |
| Chain | Residue |
| E | LEU869 |
| E | MET872 |
| E | HOH1109 |
| E | HOH1111 |
| E | HOH1132 |
| G | DG9 |
| H | DA9 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA F 1001 |
| Chain | Residue |
| F | GLU794 |
| F | ASP813 |
| F | ASP815 |
| F | ASP864 |
| F | HOH1101 |
| F | HOH1258 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K F 1002 |
| Chain | Residue |
| F | LEU869 |
| F | MET872 |
| F | HOH1114 |
| F | HOH1248 |
| G | DG9 |
| H | DA9 |
| H | HOH108 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP30 | |
| B | GLU792 | |
| B | GLU794 | |
| B | ASP813 | |
| B | ASP815 | |
| B | ASP864 | |
| E | ASP30 | |
| E | ASP77 | |
| E | GLU792 | |
| E | GLU794 | |
| E | ASP813 | |
| A | ASP77 | |
| E | ASP815 | |
| E | ASP864 | |
| F | ASP30 | |
| F | ASP77 | |
| F | GLU792 | |
| F | GLU794 | |
| F | ASP813 | |
| F | ASP815 | |
| F | ASP864 | |
| A | GLU792 | |
| A | GLU794 | |
| A | ASP813 | |
| A | ASP815 | |
| A | ASP864 | |
| B | ASP30 | |
| B | ASP77 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | SER738 | |
| B | SER738 | |
| E | SER738 | |
| F | SER738 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
