5JPI
2.15 Angstrom Crystal Structure of S-adenosylhomocysteinase from Cryptosporidium parvum in Complex with D-Eritadenine and NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004013 | molecular_function | adenosylhomocysteinase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033353 | biological_process | S-adenosylmethionine cycle |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004013 | molecular_function | adenosylhomocysteinase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0033353 | biological_process | S-adenosylmethionine cycle |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004013 | molecular_function | adenosylhomocysteinase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006730 | biological_process | one-carbon metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0033353 | biological_process | S-adenosylmethionine cycle |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004013 | molecular_function | adenosylhomocysteinase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0033353 | biological_process | S-adenosylmethionine cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | THR212 |
| A | GLU298 |
| A | ILE299 |
| A | ASP300 |
| A | CYS303 |
| A | THR331 |
| A | GLY332 |
| A | ASN333 |
| A | ILE354 |
| A | GLY355 |
| A | HIS356 |
| A | THR213 |
| A | ASN403 |
| A | HIS410 |
| A | DEA502 |
| A | HOH629 |
| A | HOH671 |
| A | HOH677 |
| A | HOH714 |
| A | HOH757 |
| A | HOH768 |
| B | LYS489 |
| A | THR214 |
| B | TYR493 |
| A | ASN246 |
| A | GLY275 |
| A | GLY277 |
| A | GLU278 |
| A | VAL279 |
| A | THR297 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue DEA A 502 |
| Chain | Residue |
| A | THR55 |
| A | GLU57 |
| A | THR58 |
| A | GLU211 |
| A | THR212 |
| A | LYS241 |
| A | ASP245 |
| A | LEU404 |
| A | THR408 |
| A | GLY409 |
| A | HIS410 |
| A | MET415 |
| A | NAD501 |
| A | HOH675 |
| A | HOH771 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | ASN260 |
| A | GLY261 |
| A | LYS378 |
| A | GLN379 |
| A | CYS406 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | LEU424 |
| A | LYS431 |
| A | LEU453 |
| A | HOH617 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | binding site for residue NAD B 501 |
| Chain | Residue |
| A | LYS489 |
| A | TYR493 |
| B | THR212 |
| B | THR213 |
| B | THR214 |
| B | ASN246 |
| B | GLY275 |
| B | GLY277 |
| B | GLU278 |
| B | VAL279 |
| B | THR297 |
| B | GLU298 |
| B | ILE299 |
| B | ASP300 |
| B | CYS303 |
| B | THR331 |
| B | GLY332 |
| B | ASN333 |
| B | ILE354 |
| B | GLY355 |
| B | HIS356 |
| B | LEU401 |
| B | ASN403 |
| B | HIS410 |
| B | DEA502 |
| B | HOH617 |
| B | HOH647 |
| B | HOH702 |
| B | HOH716 |
| B | HOH722 |
| B | HOH762 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue DEA B 502 |
| Chain | Residue |
| B | HIS53 |
| B | THR55 |
| B | GLU57 |
| B | THR58 |
| B | GLU211 |
| B | THR212 |
| B | LYS241 |
| B | ASP245 |
| B | LEU404 |
| B | THR408 |
| B | GLY409 |
| B | HIS410 |
| B | NAD501 |
| B | HOH669 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | ARG459 |
| B | LEU469 |
| B | ILE484 |
| B | ASN485 |
| B | TYR488 |
| B | HOH651 |
| B | HOH688 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | LYS36 |
| B | TYR37 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 505 |
| Chain | Residue |
| B | VAL31 |
| B | GLU32 |
| B | ARG35 |
| B | HOH659 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 506 |
| Chain | Residue |
| B | LYS431 |
| B | ARG433 |
| C | LYS431 |
| C | ARG433 |
| site_id | AD2 |
| Number of Residues | 32 |
| Details | binding site for residue NAD C 501 |
| Chain | Residue |
| C | THR212 |
| C | THR213 |
| C | THR214 |
| C | ASN246 |
| C | GLY275 |
| C | GLY277 |
| C | GLU278 |
| C | VAL279 |
| C | THR297 |
| C | GLU298 |
| C | ILE299 |
| C | ASP300 |
| C | CYS303 |
| C | THR331 |
| C | GLY332 |
| C | ASN333 |
| C | ILE354 |
| C | GLY355 |
| C | HIS356 |
| C | LEU401 |
| C | ASN403 |
| C | HIS410 |
| C | DEA502 |
| C | HOH638 |
| C | HOH669 |
| C | HOH670 |
| C | HOH742 |
| C | HOH774 |
| C | HOH814 |
| D | GLN476 |
| D | LYS489 |
| D | TYR493 |
| site_id | AD3 |
| Number of Residues | 14 |
| Details | binding site for residue DEA C 502 |
| Chain | Residue |
| C | THR55 |
| C | GLU57 |
| C | THR58 |
| C | GLU211 |
| C | THR212 |
| C | LYS241 |
| C | ASP245 |
| C | LEU404 |
| C | THR408 |
| C | GLY409 |
| C | HIS410 |
| C | MET415 |
| C | NAD501 |
| C | HOH618 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue PEG C 504 |
| Chain | Residue |
| B | GLN313 |
| C | LYS270 |
| C | ARG293 |
| C | GLN313 |
| C | VAL320 |
| C | GLU323 |
| site_id | AD5 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 C 505 |
| Chain | Residue |
| C | TRP101 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue PEG C 508 |
| Chain | Residue |
| C | LYS102 |
| C | ASN260 |
| C | GLY261 |
| C | GLN379 |
| site_id | AD7 |
| Number of Residues | 1 |
| Details | binding site for residue EDO C 509 |
| Chain | Residue |
| B | HOH729 |
| site_id | AD8 |
| Number of Residues | 34 |
| Details | binding site for residue NAD D 501 |
| Chain | Residue |
| C | GLN476 |
| C | LYS489 |
| C | TYR493 |
| D | THR212 |
| D | THR213 |
| D | THR214 |
| D | ASN246 |
| D | GLY275 |
| D | GLY277 |
| D | GLU278 |
| D | VAL279 |
| D | THR297 |
| D | GLU298 |
| D | ILE299 |
| D | ASP300 |
| D | CYS303 |
| D | THR331 |
| D | GLY332 |
| D | ASN333 |
| D | VAL336 |
| D | ILE354 |
| D | GLY355 |
| D | HIS356 |
| D | LEU401 |
| D | ASN403 |
| D | HIS410 |
| D | DEA502 |
| D | HOH657 |
| D | HOH662 |
| D | HOH689 |
| D | HOH706 |
| D | HOH722 |
| D | HOH728 |
| D | HOH826 |
| site_id | AD9 |
| Number of Residues | 16 |
| Details | binding site for residue DEA D 502 |
| Chain | Residue |
| D | HIS53 |
| D | THR55 |
| D | GLU57 |
| D | THR58 |
| D | ASP137 |
| D | GLU211 |
| D | THR212 |
| D | LYS241 |
| D | ASP245 |
| D | LEU404 |
| D | THR408 |
| D | GLY409 |
| D | HIS410 |
| D | NAD501 |
| D | HOH634 |
| D | HOH773 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 503 |
| Chain | Residue |
| D | ARG459 |
| D | ILE484 |
| D | ASN485 |
| D | TYR488 |
| D | HOH620 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue TRS D 504 |
| Chain | Residue |
| D | TYR37 |
| D | LEU424 |
| D | MET427 |
| D | ASP428 |
| D | LYS431 |
| D | HOH611 |
| site_id | AE3 |
| Number of Residues | 1 |
| Details | binding site for residue EDO D 505 |
| Chain | Residue |
| D | GLN379 |
Functional Information from PROSITE/UniProt
| site_id | PS00738 |
| Number of Residues | 15 |
| Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiYSTQDhAAAAL |
| Chain | Residue | Details |
| A | SER76-LEU90 |
| site_id | PS00739 |
| Number of Residues | 17 |
| Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKkivVlGYGeVGKGc.A |
| Chain | Residue | Details |
| A | GLY268-ALA284 |
