4B0T
Structure of the Pup Ligase PafA of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0005524 | molecular_function | ATP binding |
A | 0010498 | biological_process | proteasomal protein catabolic process |
A | 0016874 | molecular_function | ligase activity |
A | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
A | 0019787 | molecular_function | ubiquitin-like protein transferase activity |
A | 0019941 | biological_process | modification-dependent protein catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0070490 | biological_process | protein pupylation |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0005524 | molecular_function | ATP binding |
B | 0010498 | biological_process | proteasomal protein catabolic process |
B | 0016874 | molecular_function | ligase activity |
B | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
B | 0019787 | molecular_function | ubiquitin-like protein transferase activity |
B | 0019941 | biological_process | modification-dependent protein catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0070490 | biological_process | protein pupylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE ADP A 1478 |
Chain | Residue |
A | ARG60 |
A | ARG418 |
A | TRP440 |
A | PRO458 |
A | MG1479 |
A | HOH2053 |
A | HOH2250 |
A | HOH2251 |
A | HOH2252 |
B | ILE12 |
B | GLY14 |
A | THR73 |
B | ILE15 |
B | GLU16 |
B | LYS444 |
B | ASN446 |
B | PRO450 |
A | GLU75 |
A | ASN132 |
A | LEU134 |
A | ASP208 |
A | PRO210 |
A | HIS211 |
A | ARG219 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 1479 |
Chain | Residue |
A | ADP1478 |
A | HOH2053 |
A | HOH2063 |
A | HOH2250 |
A | HOH2251 |
B | GLU16 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ADP B 1479 |
Chain | Residue |
A | GLY14 |
A | ILE15 |
A | GLU16 |
A | HOH2016 |
A | HOH2235 |
A | HOH2236 |
B | ARG60 |
B | THR73 |
B | ALA74 |
B | GLU75 |
B | ASN132 |
B | LEU134 |
B | PRO210 |
B | HIS211 |
B | ARG219 |
B | ARG418 |
B | TRP440 |
B | PRO458 |
B | MG1480 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 1480 |
Chain | Residue |
A | GLU16 |
A | HOH2016 |
A | HOH2017 |
A | HOH2018 |
A | HOH2235 |
B | ADP1479 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:22910360 |
Chain | Residue | Details |
A | ASP64 | |
B | ASP64 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02111, ECO:0000269|PubMed:23601177 |
Chain | Residue | Details |
B | GLU16 | |
B | ARG60 | |
B | TYR62 | |
B | GLU70 | |
B | THR73 | |
B | TRP440 | |
A | GLU16 | |
A | ARG60 | |
A | TYR62 | |
A | GLU70 | |
A | THR73 | |
A | TRP440 |