3TWT
Crystal structure of ARC4 from human Tankyrase 2 in complex with peptide from human MCL1 (chimeric peptide)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003950 | molecular_function | NAD+ ADP-ribosyltransferase activity |
| A | 0016055 | biological_process | Wnt signaling pathway |
| A | 0032212 | biological_process | positive regulation of telomere maintenance via telomerase |
| A | 0051225 | biological_process | spindle assembly |
| B | 0003950 | molecular_function | NAD+ ADP-ribosyltransferase activity |
| B | 0016055 | biological_process | Wnt signaling pathway |
| B | 0032212 | biological_process | positive regulation of telomere maintenance via telomerase |
| B | 0051225 | biological_process | spindle assembly |
| C | 0003950 | molecular_function | NAD+ ADP-ribosyltransferase activity |
| C | 0016055 | biological_process | Wnt signaling pathway |
| C | 0032212 | biological_process | positive regulation of telomere maintenance via telomerase |
| C | 0051225 | biological_process | spindle assembly |
| D | 0003950 | molecular_function | NAD+ ADP-ribosyltransferase activity |
| D | 0016055 | biological_process | Wnt signaling pathway |
| D | 0032212 | biological_process | positive regulation of telomere maintenance via telomerase |
| D | 0051225 | biological_process | spindle assembly |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 2PE A 1 |
| Chain | Residue |
| A | TYR569 |
| E | SER13 |
| E | PHE14 |
| A | GLY570 |
| A | GLY603 |
| A | LYS604 |
| B | ASP624 |
| B | GLY625 |
| B | ASN626 |
| D | TYR572 |
| D | GLN613 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 3 |
| Chain | Residue |
| A | GLU598 |
| E | ARG6 |
| E | EDO17 |
| E | HOH136 |
| F | LEU4 |
| F | GLN5 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 5 |
| Chain | Residue |
| A | HOH29 |
| A | HOH203 |
| A | GLY570 |
| A | TYR572 |
| A | GLU573 |
| D | SO41 |
| D | HOH214 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 6 |
| Chain | Residue |
| A | ALA583 |
| A | VAL584 |
| A | VAL585 |
| A | ASN586 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 7 |
| Chain | Residue |
| A | TYR572 |
| A | GLU606 |
| A | GLN613 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 10 |
| Chain | Residue |
| A | HOH248 |
| A | HOH374 |
| A | LYS501 |
| A | TYR536 |
| A | ARG538 |
| E | GLN12 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 650 |
| Chain | Residue |
| A | LYS501 |
| A | TYR536 |
| B | LYS592 |
| B | ARG623 |
| E | GLN12 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 2 |
| Chain | Residue |
| B | HOH297 |
| B | THR619 |
| B | LYS620 |
| B | LYS621 |
| E | GLN12 |
| E | SET16 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 650 |
| Chain | Residue |
| B | HOH121 |
| B | HOH162 |
| B | HOH169 |
| B | ASN537 |
| B | GLY570 |
| B | HIS571 |
| B | TYR572 |
| B | GLU573 |
| C | HOH15 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PE8 C 2 |
| Chain | Residue |
| B | TYR572 |
| C | TYR569 |
| C | GLY570 |
| C | LYS602 |
| C | GLY603 |
| C | LYS604 |
| G | SER13 |
| G | PHE14 |
| G | HOH330 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PE8 C 3 |
| Chain | Residue |
| B | TYR605 |
| B | ASP638 |
| B | ASP641 |
| C | TYR605 |
| C | ASP638 |
| C | ASP641 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO C 1 |
| Chain | Residue |
| A | HOH343 |
| A | ASN518 |
| A | ASP551 |
| C | HOH337 |
| C | VAL579 |
| C | ALA583 |
| C | VAL584 |
| C | VAL585 |
| C | HIS614 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 8 |
| Chain | Residue |
| D | HOH49 |
| D | HOH184 |
| D | LYS501 |
| D | TYR536 |
| D | ARG538 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO D 9 |
| Chain | Residue |
| D | HOH30 |
| D | HOH171 |
| D | VAL552 |
| D | HIS553 |
| D | VAL561 |
| D | LEU563 |
| D | ALA583 |
| D | VAL584 |
| D | VAL587 |
| site_id | BC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1 |
| Chain | Residue |
| D | HOH215 |
| D | ASN537 |
| D | GLY570 |
| D | HIS571 |
| D | TYR572 |
| D | GLU573 |
| E | ARG15 |
| A | EDO5 |
| D | HOH14 |
| D | HOH67 |
| D | HOH214 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO E 17 |
| Chain | Residue |
| A | EDO3 |
| B | TRP591 |
| E | ARG6 |
| E | PRO7 |
| E | HOH136 |
| F | LEU4 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 F 17 |
| Chain | Residue |
| B | TYR569 |
| B | LYS602 |
| F | GLN12 |
| F | SER13 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 128 |
| Details | Repeat: {"description":"ANK 10"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 128 |
| Details | Repeat: {"description":"ANK 11"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 128 |
| Details | Repeat: {"description":"ANK 12"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 32 |
| Details | Region: {"description":"HIF1AN-binding","evidences":[{"source":"PubMed","id":"21251231","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"(3S)-3-hydroxyasparagine; by HIF1AN; partial","evidences":[{"source":"PubMed","id":"18936059","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"(3S)-3-hydroxyhistidine; by HIF1AN; partial","evidences":[{"source":"PubMed","id":"21251231","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
