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 | 8 |
Details | MOD_RES: (3S)-3-hydroxyasparagine; by HIF1AN; partial => ECO:0000269|PubMed:18936059 |
Chain | Residue | Details |
A | ASN518 | |
A | ASN586 | |
B | ASN518 | |
B | ASN586 | |
C | ASN518 | |
C | ASN586 | |
D | ASN518 | |
D | ASN586 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: (3S)-3-hydroxyhistidine; by HIF1AN; partial => ECO:0000269|PubMed:21251231 |
Chain | Residue | Details |
A | HIS553 | |
B | HIS553 | |
C | HIS553 | |
D | HIS553 |