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 |