1VKH
CRYSTAL STRUCTURE OF A PUTATIVE SERINE HYDROLASE (YDR428C) FROM SACCHAROMYCES CEREVISIAE AT 1.85 A RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004061 | molecular_function | arylformamidase activity |
| A | 0005575 | cellular_component | cellular_component |
| A | 0006569 | biological_process | tryptophan catabolic process |
| A | 0009435 | biological_process | NAD biosynthetic process |
| A | 0016298 | molecular_function | lipase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
| A | 0030307 | biological_process | positive regulation of cell growth |
| A | 0034354 | biological_process | 'de novo' NAD biosynthetic process from tryptophan |
| B | 0004061 | molecular_function | arylformamidase activity |
| B | 0005575 | cellular_component | cellular_component |
| B | 0006569 | biological_process | tryptophan catabolic process |
| B | 0009435 | biological_process | NAD biosynthetic process |
| B | 0016298 | molecular_function | lipase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
| B | 0030307 | biological_process | positive regulation of cell growth |
| B | 0034354 | biological_process | 'de novo' NAD biosynthetic process from tryptophan |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL B 455 |
| Chain | Residue |
| A | SER131 |
| A | GLU132 |
| A | ALA133 |
| B | SER131 |
| B | GLU132 |
| B | ALA133 |
| B | HOH547 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 456 |
| Chain | Residue |
| A | GLU30 |
| A | GLY100 |
| A | THR102 |
| A | ASN103 |
| A | THR28 |
| A | ARG29 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 457 |
| Chain | Residue |
| A | ASP228 |
| A | HOH673 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_03014 |
| Chain | Residue | Details |
| A | SER110 | |
| B | SER110 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_03014 |
| Chain | Residue | Details |
| A | ASP211 | |
| A | HIS243 | |
| B | ASP211 | |
| B | HIS243 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | SER9 | |
| B | SER9 |
