1KTG
Crystal Structure of a C. elegans Ap4A Hydrolase Binary Complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004081 | molecular_function | bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006167 | biological_process | AMP biosynthetic process |
| A | 0006172 | biological_process | ADP biosynthetic process |
| A | 0006754 | biological_process | ATP biosynthetic process |
| A | 0006915 | biological_process | apoptotic process |
| A | 0008796 | molecular_function | bis(5'-nucleosyl)-tetraphosphatase activity |
| A | 0015967 | biological_process | diadenosine tetraphosphate catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019693 | biological_process | ribose phosphate metabolic process |
| A | 0043135 | molecular_function | 5-phosphoribosyl 1-pyrophosphate pyrophosphatase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004081 | molecular_function | bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006167 | biological_process | AMP biosynthetic process |
| B | 0006172 | biological_process | ADP biosynthetic process |
| B | 0006754 | biological_process | ATP biosynthetic process |
| B | 0006915 | biological_process | apoptotic process |
| B | 0008796 | molecular_function | bis(5'-nucleosyl)-tetraphosphatase activity |
| B | 0015967 | biological_process | diadenosine tetraphosphate catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019693 | biological_process | ribose phosphate metabolic process |
| B | 0043135 | molecular_function | 5-phosphoribosyl 1-pyrophosphate pyrophosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PO4 A 402 |
| Chain | Residue |
| A | LYS36 |
| A | MG505 |
| A | OH506 |
| A | HOH715 |
| A | HOH722 |
| A | HOH732 |
| A | HOH749 |
| A | HOH756 |
| A | HOH769 |
| A | HOH827 |
| A | GLY37 |
| A | HIS38 |
| A | GLU52 |
| A | GLU56 |
| A | GLU103 |
| A | MG502 |
| A | MG503 |
| A | MG504 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PO4 B 401 |
| Chain | Residue |
| B | LYS36 |
| B | GLY37 |
| B | HIS38 |
| B | GLU52 |
| B | GLU56 |
| B | GLU103 |
| B | MG601 |
| B | MG602 |
| B | MG603 |
| B | MG604 |
| B | OH605 |
| B | HOH615 |
| B | HOH631 |
| B | HOH635 |
| B | HOH654 |
| B | HOH669 |
| B | HOH672 |
| B | HOH703 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OH A 506 |
| Chain | Residue |
| A | GLU52 |
| A | GLU103 |
| A | PO4402 |
| A | MG503 |
| A | MG504 |
| A | MG505 |
| A | HOH708 |
| A | HOH742 |
| A | HOH752 |
| A | HOH756 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OH B 605 |
| Chain | Residue |
| B | GLU52 |
| B | GLU103 |
| B | PO4401 |
| B | MG601 |
| B | MG603 |
| B | MG604 |
| B | HOH611 |
| B | HOH633 |
| B | HOH650 |
| B | HOH654 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | GLU19 |
| A | GLU111 |
| A | HOH729 |
| A | HOH737 |
| B | HOH616 |
| B | HOH638 |
| B | HOH644 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 502 |
| Chain | Residue |
| A | LYS36 |
| A | GLU56 |
| A | PO4402 |
| A | MG505 |
| A | HOH722 |
| A | HOH732 |
| A | HOH734 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG A 503 |
| Chain | Residue |
| A | GLU52 |
| A | PO4402 |
| A | MG504 |
| A | MG505 |
| A | OH506 |
| A | HOH715 |
| A | HOH752 |
| A | HOH756 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG A 504 |
| Chain | Residue |
| A | GLU103 |
| A | PO4402 |
| A | MG503 |
| A | MG505 |
| A | OH506 |
| A | HOH742 |
| A | HOH749 |
| A | HOH756 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MG A 505 |
| Chain | Residue |
| A | GLU52 |
| A | GLU56 |
| A | GLU103 |
| A | PO4402 |
| A | MG502 |
| A | MG503 |
| A | MG504 |
| A | OH506 |
| A | HOH708 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG B 601 |
| Chain | Residue |
| B | OH605 |
| B | HOH611 |
| B | HOH654 |
| B | HOH672 |
| B | GLU103 |
| B | PO4401 |
| B | MG603 |
| B | MG604 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 602 |
| Chain | Residue |
| B | LYS36 |
| B | GLU56 |
| B | PO4401 |
| B | MG603 |
| B | HOH607 |
| B | HOH615 |
| B | HOH669 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MG B 603 |
| Chain | Residue |
| B | GLU52 |
| B | GLU56 |
| B | GLU103 |
| B | PO4401 |
| B | MG601 |
| B | MG602 |
| B | MG604 |
| B | OH605 |
| B | HOH650 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG B 604 |
| Chain | Residue |
| B | GLU52 |
| B | PO4401 |
| B | MG601 |
| B | MG603 |
| B | OH605 |
| B | HOH633 |
| B | HOH635 |
| B | HOH654 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AMP A 701 |
| Chain | Residue |
| A | PRO29 |
| A | HIS31 |
| A | LYS36 |
| A | TYR76 |
| A | LYS83 |
| A | TYR121 |
| A | HOH782 |
| A | HOH843 |
Functional Information from PROSITE/UniProt
| site_id | PS00893 |
| Number of Residues | 22 |
| Details | NUDIX_BOX Nudix box signature. GhvdpgEdewqAAiRETkEEaN |
| Chain | Residue | Details |
| A | GLY37-ASN58 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 42 |
| Details | Motif: {"description":"Nudix box"} |
| Chain | Residue | Details |
