4HZF
structure of the wild type Catabolite gene Activator Protein
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0003680 | molecular_function | minor groove of adenine-thymine-rich DNA binding |
A | 0003700 | molecular_function | DNA-binding transcription factor activity |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0006351 | biological_process | DNA-templated transcription |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0008301 | molecular_function | DNA binding, bending |
A | 0030552 | molecular_function | cAMP binding |
A | 0032993 | cellular_component | protein-DNA complex |
A | 0042802 | molecular_function | identical protein binding |
A | 0043565 | molecular_function | sequence-specific DNA binding |
A | 0045013 | biological_process | carbon catabolite repression of transcription |
A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
B | 0003677 | molecular_function | DNA binding |
B | 0003680 | molecular_function | minor groove of adenine-thymine-rich DNA binding |
B | 0003700 | molecular_function | DNA-binding transcription factor activity |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0006351 | biological_process | DNA-templated transcription |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0008301 | molecular_function | DNA binding, bending |
B | 0030552 | molecular_function | cAMP binding |
B | 0032993 | cellular_component | protein-DNA complex |
B | 0042802 | molecular_function | identical protein binding |
B | 0043565 | molecular_function | sequence-specific DNA binding |
B | 0045013 | biological_process | carbon catabolite repression of transcription |
B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CMP A 301 |
Chain | Residue |
A | VAL50 |
A | ARG124 |
A | THR128 |
A | HOH401 |
A | HOH403 |
A | HOH407 |
B | LEU125 |
B | SER129 |
A | SER63 |
A | ILE71 |
A | GLY72 |
A | GLU73 |
A | LEU74 |
A | ARG83 |
A | SER84 |
A | ALA85 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CMP A 302 |
Chain | Residue |
A | LYS58 |
A | GLU59 |
A | GLN171 |
A | GLY174 |
A | GLN175 |
A | GLY178 |
A | CYS179 |
A | SER180 |
A | ARG181 |
A | HOH499 |
B | ALA136 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 A 303 |
Chain | Residue |
A | LEU106 |
A | HOH487 |
B | ASP139 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 304 |
Chain | Residue |
A | TYR64 |
A | LYS131 |
A | ASN150 |
A | GOL306 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 305 |
Chain | Residue |
A | LEU65 |
A | ASP69 |
A | GLN120 |
A | ARG124 |
A | HOH412 |
A | HOH445 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 306 |
Chain | Residue |
A | LYS131 |
A | ASN134 |
A | THR147 |
A | ILE176 |
A | GOL304 |
site_id | AC7 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE CMP B 301 |
Chain | Residue |
A | LEU125 |
A | SER129 |
B | VAL50 |
B | SER63 |
B | ILE71 |
B | GLY72 |
B | GLU73 |
B | LEU74 |
B | ARG83 |
B | SER84 |
B | ALA85 |
B | VAL87 |
B | ARG124 |
B | THR128 |
B | HOH405 |
B | HOH406 |
B | HOH425 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 302 |
Chain | Residue |
B | ALA145 |
B | LEU149 |
B | LEU196 |
B | HOH434 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 303 |
Chain | Residue |
B | CYS179 |
B | SER180 |
B | ARG181 |
B | HOH489 |
B | HOH531 |
B | HOH546 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 304 |
Chain | Residue |
B | LYS131 |
B | ASN150 |
B | GLN154 |
B | HOH476 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 305 |
Chain | Residue |
A | ARG104 |
A | GLN108 |
B | MET190 |
B | ASP193 |
Functional Information from PROSITE/UniProt
site_id | PS00042 |
Number of Residues | 24 |
Details | HTH_CRP_1 Crp-type HTH domain signature. ITRqeIGqIVGcSreTv.GRiLkmL |
Chain | Residue | Details |
A | ILE168-LEU191 |
site_id | PS00888 |
Number of Residues | 17 |
Details | CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. LIhQGEkAEtLYYIvkG |
Chain | Residue | Details |
A | LEU30-GLY46 |
site_id | PS00889 |
Number of Residues | 19 |
Details | CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. IGElGLfeegqe.....RSAwVrA |
Chain | Residue | Details |
A | ILE71-ALA89 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | DNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387 |
Chain | Residue | Details |
A | SER180-ARG186 | |
B | SER180-ARG186 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802 |
Chain | Residue | Details |
A | GLY57 | |
B | THR128 | |
B | ALA136 | |
B | GLN171 | |
A | GLY72 | |
A | ARG83 | |
A | THR128 | |
A | ALA136 | |
A | GLN171 | |
B | GLY57 | |
B | GLY72 | |
B | ARG83 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:8978616 |
Chain | Residue | Details |
A | GLU97 | |
B | GLU97 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:15520470, ECO:0000269|PubMed:8978616 |
Chain | Residue | Details |
A | LYS102 | |
B | LYS102 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
A | LYS101 | |
B | LYS101 |