2OU2
Acetyltransferase domain of Human HIV-1 Tat interacting protein, 60kDa, isoform 3
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 490 |
Chain | Residue |
A | CYS211 |
A | CYS214 |
A | HIS227 |
A | CYS231 |
site_id | AC2 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE ACO A 500 |
Chain | Residue |
A | ARG189 |
A | TRP193 |
A | PHE271 |
A | LEU272 |
A | ALA316 |
A | CYS317 |
A | ILE318 |
A | LEU319 |
A | THR320 |
A | GLN325 |
A | ARG326 |
A | ARG327 |
A | GLY328 |
A | GLY330 |
A | LYS331 |
A | GLU351 |
A | SER355 |
A | LEU357 |
A | SER361 |
A | SER364 |
A | GLN368 |
A | HOH1 |
A | HOH7 |
A | HOH25 |
A | ARG187 |
A | HIS188 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 25 |
Details | Zinc finger: {"description":"C2HC MYST-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of acetyltransferase domain of human HIV-1 TAT interacting protein in complex with acetylcoenzyme A.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q9H7Z6","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of acetyltransferase domain of human HIV-1 TAT interacting protein in complex with acetylcoenzyme A.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9H7Z6","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"24835996","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of acetyltransferase domain of human HIV-1 TAT interacting protein in complex with acetylcoenzyme A.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"17704809","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mj9 |
Chain | Residue | Details |
A | CYS317 | |
A | GLU351 |