2CG4
Structure of E.coli AsnC
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043200 | biological_process | response to amino acid |
| A | 0043565 | molecular_function | sequence-specific DNA binding |
| 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 | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043200 | biological_process | response to amino acid |
| B | 0043565 | molecular_function | sequence-specific DNA binding |
| 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 | 2 |
| Details | BINDING SITE FOR RESIDUE MG A1154 |
| Chain | Residue |
| A | ASP58 |
| B | ASP58 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ASN A1153 |
| Chain | Residue |
| A | THR136 |
| A | GLU137 |
| A | THR138 |
| A | HOH2064 |
| A | HOH2066 |
| A | TYR100 |
| A | THR101 |
| A | THR102 |
| A | GLY103 |
| A | TYR105 |
| A | SER106 |
| A | GLN128 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ASN B1153 |
| Chain | Residue |
| B | TYR100 |
| B | THR101 |
| B | THR102 |
| B | GLY103 |
| B | TYR105 |
| B | SER106 |
| B | GLN128 |
| B | THR136 |
| B | GLU137 |
| B | THR138 |
| B | HOH2059 |
| B | HOH2069 |
Functional Information from PROSITE/UniProt
| site_id | PS00519 |
| Number of Residues | 27 |
| Details | HTH_ASNC_1 AsnC-type HTH domain signature. AyaELAkqFGVSpetihvRVekMkqaG |
| Chain | Residue | Details |
| A | ALA24-GLY50 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 122 |
| Details | Domain: {"description":"HTH asnC-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00319","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 38 |
| Details | DNA binding: {"description":"H-T-H motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU00319","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
