5UJ7
Structure of the active form of human Origin Recognition Complex ATPase motor module, complex subunitS 1, 4, 5
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0005524 | molecular_function | ATP binding |
B | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0000781 | cellular_component | chromosome, telomeric region |
C | 0000808 | cellular_component | origin recognition complex |
C | 0003677 | molecular_function | DNA binding |
C | 0003688 | molecular_function | DNA replication origin binding |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005634 | cellular_component | nucleus |
C | 0005654 | cellular_component | nucleoplasm |
C | 0005664 | cellular_component | nuclear origin of replication recognition complex |
C | 0005730 | cellular_component | nucleolus |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006260 | biological_process | DNA replication |
C | 0006270 | biological_process | DNA replication initiation |
C | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0040038 | biological_process | polar body extrusion after meiotic divisions |
C | 0051258 | biological_process | protein polymerization |
D | 0000166 | molecular_function | nucleotide binding |
D | 0000781 | cellular_component | chromosome, telomeric region |
D | 0000808 | cellular_component | origin recognition complex |
D | 0003677 | molecular_function | DNA binding |
D | 0003688 | molecular_function | DNA replication origin binding |
D | 0005515 | molecular_function | protein binding |
D | 0005524 | molecular_function | ATP binding |
D | 0005634 | cellular_component | nucleus |
D | 0005654 | cellular_component | nucleoplasm |
D | 0005664 | cellular_component | nuclear origin of replication recognition complex |
D | 0005730 | cellular_component | nucleolus |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006260 | biological_process | DNA replication |
D | 0006270 | biological_process | DNA replication initiation |
D | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0040038 | biological_process | polar body extrusion after meiotic divisions |
D | 0051258 | biological_process | protein polymerization |
E | 0000808 | cellular_component | origin recognition complex |
E | 0005634 | cellular_component | nucleus |
E | 0006260 | biological_process | DNA replication |
F | 0000808 | cellular_component | origin recognition complex |
F | 0005634 | cellular_component | nucleus |
F | 0006260 | biological_process | DNA replication |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue ATP A 900 |
Chain | Residue |
A | VAL500 |
A | ASN654 |
A | TYR681 |
A | ILE689 |
A | ALA719 |
A | ARG720 |
A | LEU723 |
A | MG901 |
C | ARG209 |
A | GLU502 |
A | CYS506 |
A | PRO536 |
A | GLY539 |
A | LYS540 |
A | THR541 |
A | ALA542 |
A | GLU621 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue MG A 901 |
Chain | Residue |
A | THR541 |
A | ASP620 |
A | GLU621 |
A | ATP900 |
site_id | AC3 |
Number of Residues | 17 |
Details | binding site for residue ATP C 501 |
Chain | Residue |
C | GLN31 |
C | ASN36 |
C | PHE38 |
C | VAL40 |
C | PRO68 |
C | ARG69 |
C | GLY70 |
C | SER71 |
C | GLY72 |
C | LYS73 |
C | THR74 |
C | MET75 |
C | LEU276 |
C | ARG277 |
C | HIS280 |
C | MG502 |
E | ARG143 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue MG C 502 |
Chain | Residue |
C | THR74 |
C | ASP159 |
C | ATP501 |
E | ARG143 |
site_id | AC5 |
Number of Residues | 15 |
Details | binding site for residue ATP E 301 |
Chain | Residue |
E | LEU9 |
E | HIS38 |
E | THR39 |
E | ALA40 |
E | SER41 |
E | GLY42 |
E | LYS43 |
E | THR44 |
E | TYR45 |
E | ASP125 |
E | GLU159 |
E | TYR182 |
E | ILE190 |
E | LEU222 |
E | ARG226 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue K E 302 |
Chain | Residue |
E | PHE22 |
E | GLU24 |
E | THR119 |
E | TYR121 |
site_id | AC7 |
Number of Residues | 18 |
Details | binding site for residue ATP B 901 |
Chain | Residue |
B | VAL500 |
B | GLU502 |
B | CYS506 |
B | PRO536 |
B | GLY537 |
B | THR538 |
B | GLY539 |
B | LYS540 |
B | THR541 |
B | ALA542 |
B | GLU621 |
B | ASN654 |
B | TYR681 |
B | ILE689 |
B | ARG720 |
B | LEU723 |
B | MG902 |
D | ARG209 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue MG B 902 |
Chain | Residue |
B | THR541 |
B | ASP620 |
B | ATP901 |
site_id | AC9 |
Number of Residues | 15 |
Details | binding site for residue ATP D 501 |
Chain | Residue |
D | GLN31 |
D | PHE38 |
D | VAL40 |
D | PRO68 |
D | ARG69 |
D | GLY70 |
D | SER71 |
D | GLY72 |
D | LYS73 |
D | THR74 |
D | MET75 |
D | LEU276 |
D | ARG277 |
D | MG502 |
F | ARG143 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue MG D 502 |
Chain | Residue |
D | ATP501 |
F | ARG143 |
D | THR74 |
D | ASP159 |
site_id | AD2 |
Number of Residues | 15 |
Details | binding site for residue ATP F 301 |
Chain | Residue |
F | HIS38 |
F | THR39 |
F | ALA40 |
F | SER41 |
F | GLY42 |
F | LYS43 |
F | THR44 |
F | TYR45 |
F | ASP125 |
F | LYS126 |
F | GLU159 |
F | TYR182 |
F | ILE190 |
F | LEU222 |
F | ARG226 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue K F 302 |
Chain | Residue |
F | PHE22 |
F | GLU24 |
F | HIS27 |
F | PHE28 |
F | THR119 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
E | GLY37 | |
F | GLY37 | |
A | ARG720 | |
B | VAL500 | |
B | ASN654 | |
B | ARG720 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
C | LYS7 | |
D | LYS7 | |
A | GLU621 | |
B | GLY534 | |
B | ASP620 | |
B | GLU621 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER478 | |
B | SER478 |