4KFZ
Crystal structure of LMO2 and anti-LMO2 VH complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001221 | molecular_function | transcription coregulator binding |
A | 0003713 | molecular_function | transcription coactivator activity |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005667 | cellular_component | transcription regulator complex |
A | 0043425 | molecular_function | bHLH transcription factor binding |
A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
A | 0046872 | molecular_function | metal ion binding |
A | 0061629 | molecular_function | RNA polymerase II-specific DNA-binding transcription factor binding |
A | 0140297 | molecular_function | DNA-binding transcription factor binding |
B | 0001221 | molecular_function | transcription coregulator binding |
B | 0003713 | molecular_function | transcription coactivator activity |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005667 | cellular_component | transcription regulator complex |
B | 0043425 | molecular_function | bHLH transcription factor binding |
B | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
B | 0046872 | molecular_function | metal ion binding |
B | 0061629 | molecular_function | RNA polymerase II-specific DNA-binding transcription factor binding |
B | 0140297 | molecular_function | DNA-binding transcription factor binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 201 |
Chain | Residue |
A | CYS30 |
A | CYS33 |
A | HIS51 |
A | CYS54 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 202 |
Chain | Residue |
A | CYS57 |
A | CYS60 |
A | CYS80 |
A | ASP83 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 203 |
Chain | Residue |
A | CYS97 |
A | HIS116 |
A | CYS119 |
A | CYS94 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 204 |
Chain | Residue |
A | CYS122 |
A | CYS125 |
A | CYS144 |
A | ASP147 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 201 |
Chain | Residue |
B | CYS30 |
B | CYS33 |
B | HIS51 |
B | CYS54 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 202 |
Chain | Residue |
B | CYS57 |
B | CYS60 |
B | CYS80 |
B | ASP83 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 203 |
Chain | Residue |
B | CYS94 |
B | CYS97 |
B | HIS116 |
B | CYS119 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 204 |
Chain | Residue |
B | CYS122 |
B | CYS125 |
B | CYS144 |
B | GLN146 |
B | ASP147 |
Functional Information from PROSITE/UniProt
site_id | PS00478 |
Number of Residues | 35 |
Details | LIM_DOMAIN_1 LIM zinc-binding domain signature. CggCqqnigdryflkaidqy.....WHedClsCdlCgcrL |
Chain | Residue | Details |
A | CYS30-LEU64 | |
A | CYS94-PHE129 |