3TWV
Crystal structure of ARC4 from human Tankyrase 2 in complex with peptide from human NUMA1 (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 | 15 |
| Details | BINDING SITE FOR RESIDUE PE8 A 1 |
| Chain | Residue |
| A | HOH38 |
| D | TYR572 |
| D | GLU576 |
| D | GLU606 |
| D | GLN613 |
| E | SER13 |
| E | PHE14 |
| A | TYR569 |
| A | LYS602 |
| A | GLY603 |
| A | LYS604 |
| B | ASP624 |
| B | GLY625 |
| B | ASN626 |
| B | ASP630 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 4 |
| Chain | Residue |
| A | HOH21 |
| A | HOH140 |
| A | ARG538 |
| A | VAL539 |
| A | SER540 |
| A | VAL541 |
| D | EDO5 |
| H | ARG15 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 1 |
| Chain | Residue |
| B | GLN613 |
| B | HIS614 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 6 |
| Chain | Residue |
| B | VAL584 |
| B | VAL585 |
| B | ASN586 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PE8 C 2 |
| Chain | Residue |
| B | GLU606 |
| C | TYR569 |
| C | GLY570 |
| C | GLY603 |
| C | LYS604 |
| G | SER13 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PE8 C 3 |
| Chain | Residue |
| B | TYR605 |
| B | ASP641 |
| B | LEU642 |
| C | TYR605 |
| C | ASP638 |
| C | ASP641 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 650 |
| Chain | Residue |
| B | GLY635 |
| B | THR637 |
| C | LYS609 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 6 |
| Chain | Residue |
| C | LYS592 |
| C | ARG623 |
| D | GLU491 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 4 |
| Chain | Residue |
| C | GLN515 |
| D | HIS553 |
| D | VAL561 |
| D | VAL584 |
| D | VAL587 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 5 |
| Chain | Residue |
| A | SO44 |
| A | SER540 |
| D | HOH100 |
| D | ARG538 |
| H | ARG15 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1 |
| Chain | Residue |
| A | HOH21 |
| D | ASN537 |
| D | ARG538 |
| D | VAL539 |
| D | SER540 |
| E | ARG15 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 7 |
| Chain | Residue |
| C | SER490 |
| C | GLU491 |
| D | LYS592 |
| D | ARG623 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 F 17 |
| Chain | Residue |
| B | TYR569 |
| B | LYS602 |
| F | GLN12 |
| F | SER13 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO G 17 |
| Chain | Residue |
| C | TYR569 |
| G | SER13 |
| G | HOH137 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 G 18 |
| Chain | Residue |
| B | HOH7 |
| B | ASN537 |
| B | GLY570 |
| B | TYR572 |
| B | GLU573 |
| C | HOH19 |
| G | ARG15 |
| G | HOH138 |
| G | HOH139 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 H 17 |
| Chain | Residue |
| D | TYR569 |
| D | LYS602 |
| H | GLN8 |
| H | GLN12 |
| H | SER13 |
| H | HOH37 |
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 |
