2HCB
Structure of AMPPCP-bound DnaA from Aquifex aeolicus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0003688 | molecular_function | DNA replication origin binding |
A | 0005524 | molecular_function | ATP binding |
A | 0006270 | biological_process | DNA replication initiation |
A | 0006275 | biological_process | regulation of DNA replication |
A | 0043565 | molecular_function | sequence-specific DNA binding |
B | 0003677 | molecular_function | DNA binding |
B | 0003688 | molecular_function | DNA replication origin binding |
B | 0005524 | molecular_function | ATP binding |
B | 0006270 | biological_process | DNA replication initiation |
B | 0006275 | biological_process | regulation of DNA replication |
B | 0043565 | molecular_function | sequence-specific DNA binding |
C | 0003677 | molecular_function | DNA binding |
C | 0003688 | molecular_function | DNA replication origin binding |
C | 0005524 | molecular_function | ATP binding |
C | 0006270 | biological_process | DNA replication initiation |
C | 0006275 | biological_process | regulation of DNA replication |
C | 0043565 | molecular_function | sequence-specific DNA binding |
D | 0003677 | molecular_function | DNA binding |
D | 0003688 | molecular_function | DNA replication origin binding |
D | 0005524 | molecular_function | ATP binding |
D | 0006270 | biological_process | DNA replication initiation |
D | 0006275 | biological_process | regulation of DNA replication |
D | 0043565 | molecular_function | sequence-specific DNA binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 400 |
Chain | Residue |
A | THR126 |
A | ASP180 |
A | ASP181 |
A | ACP700 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 401 |
Chain | Residue |
B | THR126 |
B | ASP181 |
B | ACP700 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 402 |
Chain | Residue |
C | ASP181 |
C | ACP700 |
C | LYS125 |
C | THR126 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 403 |
Chain | Residue |
D | LYS125 |
D | THR126 |
D | ASP180 |
D | ASP181 |
D | ACP700 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE ACP A 700 |
Chain | Residue |
A | TYR83 |
A | PHE88 |
A | ILE89 |
A | ASN94 |
A | VAL121 |
A | GLY122 |
A | THR123 |
A | GLY124 |
A | LYS125 |
A | THR126 |
A | HIS127 |
A | ASP181 |
A | VAL276 |
A | ARG277 |
A | GLU280 |
A | MG400 |
D | ARG230 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ACP B 700 |
Chain | Residue |
A | ARG230 |
B | TYR83 |
B | ASN87 |
B | PHE88 |
B | ILE89 |
B | ASN94 |
B | VAL121 |
B | GLY122 |
B | THR123 |
B | GLY124 |
B | LYS125 |
B | THR126 |
B | HIS127 |
B | ASP181 |
B | LYS253 |
B | VAL276 |
B | ARG277 |
B | GLU280 |
B | MG401 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ACP C 700 |
Chain | Residue |
B | ARG230 |
C | ASN87 |
C | PHE88 |
C | ILE89 |
C | ASN94 |
C | VAL121 |
C | GLY122 |
C | THR123 |
C | GLY124 |
C | LYS125 |
C | THR126 |
C | HIS127 |
C | ASP181 |
C | LYS253 |
C | VAL276 |
C | ARG277 |
C | GLU280 |
C | MG402 |
site_id | AC8 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE ACP D 700 |
Chain | Residue |
C | ARG230 |
D | PHE88 |
D | ILE89 |
D | ASN94 |
D | VAL121 |
D | GLY122 |
D | THR123 |
D | GLY124 |
D | LYS125 |
D | THR126 |
D | HIS127 |
D | ASP181 |
D | LYS253 |
D | VAL276 |
D | ARG277 |
D | GLU280 |
D | MG403 |
Functional Information from PROSITE/UniProt
site_id | PS01008 |
Number of Residues | 20 |
Details | DNAA DnaA protein signature. IAraFKrKdHTTVihAirsV |
Chain | Residue | Details |
A | ILE354-VAL373 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305|PubMed:16829961, ECO:0007744|PDB:2HCB, ECO:0007744|PDB:3R8F |
Chain | Residue | Details |
A | ILE89 | |
D | ILE89 | |
D | HIS127 | |
D | ARG277 | |
A | HIS127 | |
A | ARG277 | |
B | ILE89 | |
B | HIS127 | |
B | ARG277 | |
C | ILE89 | |
C | HIS127 | |
C | ARG277 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12234917, ECO:0007744|PDB:1L8Q |
Chain | Residue | Details |
A | ASN94 | |
A | THR123 | |
B | ASN94 | |
B | THR123 | |
C | ASN94 | |
C | THR123 | |
D | ASN94 | |
D | THR123 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00377, ECO:0000305|PubMed:16829961, ECO:0007744|PDB:2HCB |
Chain | Residue | Details |
A | GLY122 | |
B | GLY122 | |
C | GLY122 | |
D | GLY122 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00377, ECO:0000305|PubMed:16829961, ECO:0007744|PDB:2HCB, ECO:0007744|PDB:3R8F |
Chain | Residue | Details |
A | GLY124 | |
A | LYS125 | |
B | GLY124 | |
B | LYS125 | |
C | GLY124 | |
C | LYS125 | |
D | GLY124 | |
D | LYS125 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0007744|PDB:1L8Q, ECO:0007744|PDB:2HCB, ECO:0007744|PDB:3R8F |
Chain | Residue | Details |
A | THR126 | |
B | THR126 | |
C | THR126 | |
D | THR126 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21964332 |
Chain | Residue | Details |
A | VAL156 | |
B | VAL156 | |
C | VAL156 | |
D | VAL156 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0007744|PDB:3R8F |
Chain | Residue | Details |
A | ASP180 | |
B | ASP180 | |
C | ASP180 | |
D | ASP180 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0007744|PDB:2HCB, ECO:0007744|PDB:3R8F |
Chain | Residue | Details |
A | ASP181 | |
B | ASP181 | |
C | ASP181 | |
D | ASP181 |
site_id | SWS_FT_FI9 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21964332, ECO:0007744|PDB:3R8F |
Chain | Residue | Details |
A | LYS188 | |
D | LYS188 | |
D | ARG190 | |
D | THR191 | |
A | ARG190 | |
A | THR191 | |
B | LYS188 | |
B | ARG190 | |
B | THR191 | |
C | LYS188 | |
C | ARG190 | |
C | THR191 |