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 |