5TLS
2.4 Angstrom Crystal Structure of S-adenosylhomocysteinase from Cryptosporidium parvum in Complex with DZ2002 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 | ALA330 |
| A | THR331 |
| A | GLY332 |
| A | ASN333 |
| A | ILE354 |
| A | GLY355 |
| A | THR213 |
| A | HIS356 |
| A | ASN403 |
| A | HIS410 |
| A | ZD2502 |
| A | HOH614 |
| A | HOH682 |
| A | HOH765 |
| A | HOH783 |
| B | GLN476 |
| B | LYS489 |
| A | THR214 |
| B | TYR493 |
| A | ASN246 |
| A | GLY275 |
| A | GLY277 |
| A | GLU278 |
| A | VAL279 |
| A | THR297 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue ZD2 A 502 |
| Chain | Residue |
| A | HIS53 |
| A | THR55 |
| A | GLU57 |
| A | THR58 |
| A | ASP137 |
| A | GLU211 |
| A | THR212 |
| A | LYS241 |
| A | ASP245 |
| A | LEU404 |
| A | THR408 |
| A | GLY409 |
| A | HIS410 |
| A | MET415 |
| A | NAD501 |
| A | HOH662 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | LYS431 |
| A | ARG433 |
| C | LYS431 |
| C | ARG433 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 A 504 |
| Chain | Residue |
| A | TRP101 |
| B | ARG35 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 505 |
| Chain | Residue |
| A | LYS270 |
| A | ARG293 |
| A | GLU323 |
| A | HOH698 |
| C | GLN313 |
| C | HOH725 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 A 506 |
| Chain | Residue |
| A | LEU453 |
| A | TYR456 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 A 507 |
| Chain | Residue |
| A | ASN481 |
| A | VAL482 |
| A | SER483 |
| A | HOH746 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 A 508 |
| Chain | Residue |
| A | MET427 |
| A | HOH611 |
| site_id | AC9 |
| Number of Residues | 32 |
| Details | binding site for residue NAD B 501 |
| Chain | Residue |
| A | GLN476 |
| 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 | ALA330 |
| B | THR331 |
| B | GLY332 |
| B | ASN333 |
| B | ILE354 |
| B | GLY355 |
| B | HIS356 |
| B | ASN403 |
| B | HIS410 |
| B | ZD2502 |
| B | HOH613 |
| B | HOH665 |
| B | HOH724 |
| B | HOH730 |
| B | HOH733 |
| B | HOH762 |
| site_id | AD1 |
| Number of Residues | 16 |
| Details | binding site for residue ZD2 B 502 |
| Chain | Residue |
| B | THR55 |
| B | GLU57 |
| B | THR58 |
| B | ASP137 |
| B | GLU211 |
| B | THR212 |
| B | LYS241 |
| B | ASP245 |
| B | LEU404 |
| B | THR408 |
| B | GLY409 |
| B | HIS410 |
| B | MET415 |
| B | NAD501 |
| B | HOH630 |
| B | HIS53 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 B 504 |
| Chain | Residue |
| B | ARG35 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 505 |
| Chain | Residue |
| B | LYS270 |
| B | ARG293 |
| B | GLU323 |
| B | HOH625 |
| D | GLN313 |
| D | HOH708 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 B 506 |
| Chain | Residue |
| B | TYR456 |
| site_id | AD5 |
| Number of Residues | 29 |
| 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 | ASN403 |
| C | HIS410 |
| C | ZD2502 |
| C | HOH645 |
| C | HOH706 |
| C | HOH715 |
| C | HOH762 |
| C | HOH768 |
| D | LYS489 |
| D | TYR493 |
| site_id | AD6 |
| Number of Residues | 16 |
| Details | binding site for residue ZD2 C 502 |
| Chain | Residue |
| C | HIS53 |
| C | THR55 |
| C | GLU57 |
| C | THR58 |
| C | ASP137 |
| C | GLU211 |
| C | THR212 |
| C | LYS241 |
| C | ASP245 |
| C | LEU404 |
| C | THR408 |
| C | GLY409 |
| C | HIS410 |
| C | MET415 |
| C | NAD501 |
| C | HOH685 |
| site_id | AD7 |
| Number of Residues | 1 |
| Details | binding site for residue GOL C 503 |
| Chain | Residue |
| C | TYR37 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 C 504 |
| Chain | Residue |
| A | GLN313 |
| C | LYS270 |
| C | ARG293 |
| C | GLU323 |
| C | HOH602 |
| C | HOH725 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 C 506 |
| Chain | Residue |
| C | THR214 |
| C | ARG218 |
| C | HOH606 |
| D | TYR479 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 C 507 |
| Chain | Residue |
| A | LYS125 |
| A | LYS127 |
| C | ARG343 |
| C | HOH655 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 C 508 |
| Chain | Residue |
| C | ARG38 |
| C | HOH655 |
| site_id | AE3 |
| Number of Residues | 32 |
| 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 | ALA330 |
| D | THR331 |
| D | GLY332 |
| D | ASN333 |
| D | ILE354 |
| D | GLY355 |
| D | HIS356 |
| D | LEU401 |
| D | ASN403 |
| D | HIS410 |
| D | ZD2502 |
| D | HOH647 |
| D | HOH665 |
| D | HOH674 |
| D | HOH691 |
| D | HOH720 |
| site_id | AE4 |
| Number of Residues | 15 |
| Details | binding site for residue ZD2 D 502 |
| Chain | Residue |
| D | HIS53 |
| D | THR55 |
| D | GLU57 |
| D | THR58 |
| D | GLU211 |
| D | THR212 |
| D | LYS241 |
| D | ASP245 |
| D | LEU404 |
| D | THR408 |
| D | GLY409 |
| D | HIS410 |
| D | MET415 |
| D | NAD501 |
| D | HOH627 |
| site_id | AE5 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 D 503 |
| Chain | Residue |
| B | GLN313 |
| D | LYS270 |
| D | ARG293 |
| D | GLU323 |
| D | HOH609 |
| D | HOH612 |
| D | HOH708 |
| site_id | AE6 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 D 504 |
| Chain | Residue |
| D | TRP101 |
| site_id | AE7 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 D 505 |
| Chain | Residue |
| D | ASN481 |
| D | VAL482 |
| site_id | AE8 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 D 506 |
| Chain | Residue |
| D | TYR80 |
| D | GLU367 |
| D | LYS398 |
| D | ARG400 |
| D | HOH729 |
| D | HOH750 |
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 |
