1Z6R
Crystal structure of Mlc from Escherichia coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006351 | biological_process | DNA-templated transcription |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0016020 | cellular_component | membrane |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0003677 | molecular_function | DNA binding |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006351 | biological_process | DNA-templated transcription |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0016020 | cellular_component | membrane |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
C | 0003677 | molecular_function | DNA binding |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006351 | biological_process | DNA-templated transcription |
C | 0006355 | biological_process | regulation of DNA-templated transcription |
C | 0016020 | cellular_component | membrane |
C | 0042802 | molecular_function | identical protein binding |
C | 0046872 | molecular_function | metal ion binding |
D | 0003677 | molecular_function | DNA binding |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006351 | biological_process | DNA-templated transcription |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0016020 | cellular_component | membrane |
D | 0042802 | molecular_function | identical protein binding |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 501 |
Chain | Residue |
A | HIS247 |
A | CYS257 |
A | CYS259 |
A | CYS264 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 502 |
Chain | Residue |
B | HIS247 |
B | CYS257 |
B | CYS259 |
B | CYS264 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 503 |
Chain | Residue |
C | CYS257 |
C | CYS259 |
C | CYS264 |
C | HIS247 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 504 |
Chain | Residue |
D | HIS247 |
D | CYS257 |
D | CYS259 |
D | CYS264 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 36 |
Details | DNA_BIND: H-T-H motif => ECO:0000250 |
Chain | Residue | Details |
A | ARG33-LEU42 | |
B | ARG33-LEU42 | |
C | ARG33-LEU42 | |
D | ARG33-LEU42 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15929984, ECO:0000269|PubMed:18319344, ECO:0007744|PDB:1Z6R, ECO:0007744|PDB:3BP8 |
Chain | Residue | Details |
A | HIS247 | |
C | CYS257 | |
C | CYS259 | |
C | CYS264 | |
D | HIS247 | |
D | CYS257 | |
D | CYS259 | |
D | CYS264 | |
A | CYS257 | |
A | CYS259 | |
A | CYS264 | |
B | HIS247 | |
B | CYS257 | |
B | CYS259 | |
B | CYS264 | |
C | HIS247 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1q18 |
Chain | Residue | Details |
A | ASP195 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1q18 |
Chain | Residue | Details |
B | ASP195 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1q18 |
Chain | Residue | Details |
C | ASP195 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1q18 |
Chain | Residue | Details |
D | ASP195 |