2CA9
apo-NIKR from helicobacter pylori in closed trans-conformation
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000976 | molecular_function | transcription cis-regulatory region binding |
A | 0001217 | molecular_function | DNA-binding transcription repressor activity |
A | 0003677 | molecular_function | DNA binding |
A | 0003700 | molecular_function | DNA-binding transcription factor activity |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0010045 | biological_process | response to nickel cation |
A | 0016151 | molecular_function | nickel cation binding |
A | 0032993 | cellular_component | protein-DNA complex |
A | 0042802 | molecular_function | identical protein binding |
A | 0043565 | molecular_function | sequence-specific DNA binding |
A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
A | 0046872 | molecular_function | metal ion binding |
B | 0000976 | molecular_function | transcription cis-regulatory region binding |
B | 0001217 | molecular_function | DNA-binding transcription repressor activity |
B | 0003677 | molecular_function | DNA binding |
B | 0003700 | molecular_function | DNA-binding transcription factor activity |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0010045 | biological_process | response to nickel cation |
B | 0016151 | molecular_function | nickel cation binding |
B | 0032993 | cellular_component | protein-DNA complex |
B | 0042802 | molecular_function | identical protein binding |
B | 0043565 | molecular_function | sequence-specific DNA binding |
B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 1147 |
Chain | Residue |
A | TYR72 |
A | HIS74 |
A | ASN80 |
A | HOH2037 |
B | HIS88 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT A 1148 |
Chain | Residue |
A | GOL1152 |
A | GOL1152 |
A | ARG82 |
A | ARG82 |
A | ARG131 |
A | ARG131 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT A 1149 |
Chain | Residue |
A | LYS137 |
A | LEU138 |
B | LEU138 |
B | THR139 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 1150 |
Chain | Residue |
A | HIS74 |
A | HIS75 |
A | HOH2064 |
A | HOH2065 |
B | HIS88 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 1151 |
Chain | Residue |
A | GLU78 |
A | GLN81 |
A | ARG82 |
A | LEU130 |
A | HOH2030 |
A | HOH2030 |
A | HOH2066 |
B | ARG77 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 1152 |
Chain | Residue |
A | ARG82 |
A | GLY129 |
A | LEU130 |
A | ARG131 |
A | FMT1148 |
A | FMT1148 |
A | HOH2067 |
A | HOH2068 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT B 1148 |
Chain | Residue |
A | LYS31 |
B | ARG82 |
B | ILE86 |
B | HOH2033 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT B 1149 |
Chain | Residue |
B | TYR72 |
B | HIS99 |
B | HIS101 |
B | HOH2019 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FMT B 1150 |
Chain | Residue |
A | TYR34 |
A | LEU40 |
B | LYS48 |
B | ASP52 |
B | GLY129 |
B | HOH2011 |
B | HOH2059 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 1151 |
Chain | Residue |
B | ASN80 |
B | MET83 |
B | GLN87 |
B | GLU109 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00476","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |