3D64
Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia pseudomallei
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004013 | molecular_function | adenosylhomocysteinase activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 |
| A | 0071269 | biological_process | L-homocysteine biosynthetic process |
| B | 0004013 | molecular_function | adenosylhomocysteinase activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 |
| B | 0071269 | biological_process | L-homocysteine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD B 601 |
| Chain | Residue |
| A | LYS467 |
| B | ASP288 |
| B | CYS291 |
| B | THR319 |
| B | GLY320 |
| B | ASN321 |
| B | ILE342 |
| B | GLY343 |
| B | HIS344 |
| B | ASN387 |
| A | TYR471 |
| B | ASP233 |
| B | ASN234 |
| B | GLY265 |
| B | ASP266 |
| B | THR285 |
| B | GLU286 |
| B | ILE287 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD A 601 |
| Chain | Residue |
| A | ASP233 |
| A | ASN234 |
| A | GLY265 |
| A | ASP266 |
| A | THR285 |
| A | GLU286 |
| A | ILE287 |
| A | ASP288 |
| A | CYS291 |
| A | ALA318 |
| A | THR319 |
| A | GLY320 |
| A | ASN321 |
| A | ILE342 |
| A | GLY343 |
| A | HIS344 |
| A | LEU385 |
| A | ASN387 |
| B | LYS467 |
| B | TYR471 |
Functional Information from PROSITE/UniProt
| site_id | PS00738 |
| Number of Residues | 15 |
| Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQDhAAAAI |
| Chain | Residue | Details |
| A | SER85-ILE99 |
| site_id | PS00739 |
| Number of Residues | 17 |
| Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKiavVaGYGdVGKGc.A |
| Chain | Residue | Details |
| A | GLY256-ALA272 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00563","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00563","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia pseudomallei.","authoringGroup":["Seattle structural genomics center for infectious disease (SSGCID)"]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of S-adenosyl-l-homocysteine hydrolase from Burkholderia pseudomallei in complex with 9-beta-D-arabino-furanosyl-adenine.","authoringGroup":["Joint center for structural genomics (JCSG)"]}}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| A | LYS229 | |
| A | ASN234 | |
| A | CYS238 | |
| A | HIS62 | |
| A | ASP139 | |
| A | HIS344 | |
| A | ASP233 |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| B | LYS229 | |
| B | ASN234 | |
| B | CYS238 | |
| B | HIS62 | |
| B | ASP139 | |
| B | HIS344 | |
| B | ASP233 |
