2B5U
Crystal Structure Of Colicin E3 V206C Mutant In Complex With Its Immunity Protein
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000049 | molecular_function | tRNA binding |
A | 0003723 | molecular_function | RNA binding |
A | 0004519 | molecular_function | endonuclease activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005727 | cellular_component | extrachromosomal circular DNA |
A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
A | 0016829 | molecular_function | lyase activity |
A | 0019843 | molecular_function | rRNA binding |
A | 0031640 | biological_process | killing of cells of another organism |
A | 0032413 | biological_process | negative regulation of ion transmembrane transporter activity |
A | 0042742 | biological_process | defense response to bacterium |
A | 0043022 | molecular_function | ribosome binding |
A | 0044325 | molecular_function | transmembrane transporter binding |
B | 0005515 | molecular_function | protein binding |
B | 0015643 | molecular_function | toxic substance binding |
B | 0030153 | biological_process | bacteriocin immunity |
C | 0000049 | molecular_function | tRNA binding |
C | 0003723 | molecular_function | RNA binding |
C | 0004519 | molecular_function | endonuclease activity |
C | 0005515 | molecular_function | protein binding |
C | 0005576 | cellular_component | extracellular region |
C | 0005727 | cellular_component | extrachromosomal circular DNA |
C | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
C | 0016829 | molecular_function | lyase activity |
C | 0019843 | molecular_function | rRNA binding |
C | 0031640 | biological_process | killing of cells of another organism |
C | 0032413 | biological_process | negative regulation of ion transmembrane transporter activity |
C | 0042742 | biological_process | defense response to bacterium |
C | 0043022 | molecular_function | ribosome binding |
C | 0044325 | molecular_function | transmembrane transporter binding |
D | 0005515 | molecular_function | protein binding |
D | 0015643 | molecular_function | toxic substance binding |
D | 0030153 | biological_process | bacteriocin immunity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CIT C 601 |
Chain | Residue |
C | ARG495 |
C | TYR519 |
C | LYS544 |
C | ARG545 |
C | ASN546 |
C | HOH670 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CIT A 602 |
Chain | Residue |
A | ASN546 |
A | TYR550 |
A | HOH699 |
A | ARG495 |
A | TYR519 |
A | ARG545 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642 |
Chain | Residue | Details |
A | HIS513 | |
C | HIS513 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642 |
Chain | Residue | Details |
A | GLU517 | |
C | GLU517 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:11741540 |
Chain | Residue | Details |
A | ARG545 | |
C | ARG545 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Stabilizes positive charge on His-513 => ECO:0000305|PubMed:20852642 |
Chain | Residue | Details |
A | ASP510 | |
C | ASP510 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1jch |
Chain | Residue | Details |
A | ASP510 | |
A | HIS513 | |
A | ARG545 | |
A | GLU517 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1jch |
Chain | Residue | Details |
C | ASP510 | |
C | HIS513 | |
C | ARG545 | |
C | GLU517 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 530 |
Chain | Residue | Details |
A | ASP510 | electrostatic stabiliser, increase acidity |
A | HIS513 | promote heterolysis, proton acceptor, proton donor |
A | GLU517 | increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
A | ARG545 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 530 |
Chain | Residue | Details |
C | ASP510 | electrostatic stabiliser, increase acidity |
C | HIS513 | promote heterolysis, proton acceptor, proton donor |
C | GLU517 | increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
C | ARG545 | electrostatic stabiliser |