1V8B
Crystal structure of a hydrolase
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 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 | 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 | 31 |
Details | BINDING SITE FOR RESIDUE NAD A 501 |
Chain | Residue |
A | THR201 |
A | GLU287 |
A | ILE288 |
A | ASP289 |
A | CYS292 |
A | CYS319 |
A | THR320 |
A | GLY321 |
A | ASN322 |
A | ILE343 |
A | GLY344 |
A | THR202 |
A | HIS345 |
A | LEU389 |
A | ASN391 |
A | HIS398 |
A | ADN502 |
A | HOH504 |
A | HOH523 |
A | HOH533 |
A | HOH576 |
B | GLN460 |
A | THR203 |
B | LYS473 |
B | TYR477 |
A | ASN235 |
A | GLY264 |
A | GLY266 |
A | ASP267 |
A | VAL268 |
A | THR286 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ADN A 502 |
Chain | Residue |
A | HIS54 |
A | THR56 |
A | GLU58 |
A | ASP134 |
A | GLU200 |
A | THR201 |
A | LYS230 |
A | ASP234 |
A | LEU389 |
A | THR396 |
A | HIS398 |
A | MET403 |
A | NAD501 |
site_id | AC3 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD B 501 |
Chain | Residue |
A | GLN460 |
A | LYS473 |
A | TYR477 |
B | THR201 |
B | THR202 |
B | THR203 |
B | ASN235 |
B | GLY264 |
B | GLY266 |
B | ASP267 |
B | VAL268 |
B | THR286 |
B | GLU287 |
B | ILE288 |
B | ASP289 |
B | CYS292 |
B | CYS319 |
B | THR320 |
B | GLY321 |
B | ASN322 |
B | ILE343 |
B | GLY344 |
B | HIS345 |
B | LEU389 |
B | ASN391 |
B | HIS398 |
B | ADN1502 |
B | HOH1503 |
B | HOH1546 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ADN B 1502 |
Chain | Residue |
B | HIS54 |
B | THR56 |
B | GLU58 |
B | ASP134 |
B | GLU200 |
B | THR201 |
B | LYS230 |
B | ASP234 |
B | LEU389 |
B | THR396 |
B | HIS398 |
B | MET403 |
B | NAD501 |
B | HOH1537 |
site_id | AC5 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAD C 501 |
Chain | Residue |
C | CYS292 |
C | CYS319 |
C | THR320 |
C | GLY321 |
C | ASN322 |
C | ILE343 |
C | GLY344 |
C | HIS345 |
C | LEU389 |
C | ASN391 |
C | HIS398 |
C | ADN2502 |
C | HOH2519 |
C | HOH2525 |
C | HOH2529 |
C | HOH2536 |
C | HOH2549 |
D | GLN460 |
D | LYS473 |
D | TYR477 |
C | THR201 |
C | THR202 |
C | THR203 |
C | ASN235 |
C | GLY264 |
C | GLY266 |
C | ASP267 |
C | VAL268 |
C | THR286 |
C | GLU287 |
C | ILE288 |
C | ASP289 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADN C 2502 |
Chain | Residue |
C | LEU53 |
C | HIS54 |
C | THR56 |
C | GLU58 |
C | ASP134 |
C | GLU200 |
C | THR201 |
C | LYS230 |
C | ASP234 |
C | LEU389 |
C | THR396 |
C | HIS398 |
C | MET403 |
C | PHE407 |
C | NAD501 |
site_id | AC7 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAD D 501 |
Chain | Residue |
C | GLN460 |
C | LYS473 |
C | TYR477 |
D | THR201 |
D | THR202 |
D | THR203 |
D | ASN235 |
D | GLY264 |
D | GLY266 |
D | ASP267 |
D | VAL268 |
D | THR286 |
D | GLU287 |
D | ILE288 |
D | ASP289 |
D | CYS292 |
D | CYS319 |
D | THR320 |
D | GLY321 |
D | ASN322 |
D | ILE343 |
D | GLY344 |
D | HIS345 |
D | LEU389 |
D | ASN391 |
D | HIS398 |
D | ADN3502 |
D | HOH3549 |
D | HOH3579 |
D | HOH3597 |
site_id | AC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADN D 3502 |
Chain | Residue |
D | HIS54 |
D | THR56 |
D | GLU58 |
D | ASP134 |
D | GLU200 |
D | THR201 |
D | LYS230 |
D | ASP234 |
D | LEU389 |
D | THR396 |
D | GLY397 |
D | HIS398 |
D | MET403 |
D | NAD501 |
D | HOH3547 |
Functional Information from PROSITE/UniProt
site_id | PS00738 |
Number of Residues | 15 |
Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiYSTADyAAAAV |
Chain | Residue | Details |
A | SER77-VAL91 |
site_id | PS00739 |
Number of Residues | 18 |
Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKivvIcGYGdVGKGcaS |
Chain | Residue | Details |
A | GLY257-SER274 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | BINDING: |
Chain | Residue | Details |
A | THR56 | |
B | ASP234 | |
C | THR56 | |
C | ASP134 | |
C | GLU200 | |
C | LYS230 | |
C | ASP234 | |
D | THR56 | |
D | ASP134 | |
D | GLU200 | |
D | LYS230 | |
A | ASP134 | |
D | ASP234 | |
A | GLU200 | |
A | LYS230 | |
A | ASP234 | |
B | THR56 | |
B | ASP134 | |
B | GLU200 | |
B | LYS230 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15476817 |
Chain | Residue | Details |
A | THR201 | |
B | GLY264 | |
B | GLU287 | |
B | ASN322 | |
B | ILE343 | |
B | ASN391 | |
C | THR201 | |
C | ASN235 | |
C | GLY264 | |
C | GLU287 | |
C | ASN322 | |
A | ASN235 | |
C | ILE343 | |
C | ASN391 | |
D | THR201 | |
D | ASN235 | |
D | GLY264 | |
D | GLU287 | |
D | ASN322 | |
D | ILE343 | |
D | ASN391 | |
A | GLY264 | |
A | GLU287 | |
A | ASN322 | |
A | ILE343 | |
A | ASN391 | |
B | THR201 | |
B | ASN235 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Important for nucleoside inhibitor binding |
Chain | Residue | Details |
A | CYS59 | |
B | CYS59 | |
C | CYS59 | |
D | CYS59 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 7 |
Details | Annotated By Reference To The Literature 1b3r |
Chain | Residue | Details |
A | HIS54 | |
A | HIS345 | |
A | ASP234 | |
A | ASP134 | |
A | CYS239 | |
A | LYS230 | |
A | ASN235 |
site_id | CSA2 |
Number of Residues | 7 |
Details | Annotated By Reference To The Literature 1b3r |
Chain | Residue | Details |
B | HIS54 | |
B | HIS345 | |
B | ASP234 | |
B | ASP134 | |
B | CYS239 | |
B | LYS230 | |
B | ASN235 |
site_id | CSA3 |
Number of Residues | 7 |
Details | Annotated By Reference To The Literature 1b3r |
Chain | Residue | Details |
C | HIS54 | |
C | HIS345 | |
C | ASP234 | |
C | ASP134 | |
C | CYS239 | |
C | LYS230 | |
C | ASN235 |
site_id | CSA4 |
Number of Residues | 7 |
Details | Annotated By Reference To The Literature 1b3r |
Chain | Residue | Details |
D | HIS54 | |
D | HIS345 | |
D | ASP234 | |
D | ASP134 | |
D | CYS239 | |
D | LYS230 | |
D | ASN235 |