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 | 0035162 | biological_process | embryonic hemopoiesis |
| 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 |
| 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 | 0035162 | biological_process | embryonic hemopoiesis |
| 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 |
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 118 |
| Details | Domain: {"description":"LIM zinc-binding 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00125","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 118 |
| Details | Domain: {"description":"LIM zinc-binding 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00125","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 194 |
| Details | Domain: {"description":"Ig-like"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 48 |
| Details | Region: {"description":"Framework-1","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | Region: {"description":"Complementarity-determining-1","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 32 |
| Details | Region: {"description":"Framework-2","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 14 |
| Details | Region: {"description":"Complementarity-determining-2","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 74 |
| Details | Region: {"description":"Framework-3","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Region: {"description":"Complementarity-determining-3","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
