2ZSU
Crystal structure of spermidine synthase from Pyrococcus horikoshii OT3, P1 form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004766 | molecular_function | spermidine synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006596 | biological_process | polyamine biosynthetic process |
| A | 0008295 | biological_process | spermidine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004766 | molecular_function | spermidine synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006596 | biological_process | polyamine biosynthetic process |
| B | 0008295 | biological_process | spermidine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004766 | molecular_function | spermidine synthase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006596 | biological_process | polyamine biosynthetic process |
| C | 0008295 | biological_process | spermidine biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004766 | molecular_function | spermidine synthase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006596 | biological_process | polyamine biosynthetic process |
| D | 0008295 | biological_process | spermidine biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004766 | molecular_function | spermidine synthase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006596 | biological_process | polyamine biosynthetic process |
| E | 0008295 | biological_process | spermidine biosynthetic process |
| E | 0016740 | molecular_function | transferase activity |
| E | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004766 | molecular_function | spermidine synthase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006596 | biological_process | polyamine biosynthetic process |
| F | 0008295 | biological_process | spermidine biosynthetic process |
| F | 0016740 | molecular_function | transferase activity |
| F | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AG3 A1001 |
| Chain | Residue |
| A | GLU8 |
| A | THR163 |
| A | ASP164 |
| A | TYR229 |
| A | TRP233 |
| A | TYR10 |
| A | VAL52 |
| A | GLN53 |
| A | TYR62 |
| A | HIS63 |
| A | ASP87 |
| A | ASP161 |
| A | SER162 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AG3 C1002 |
| Chain | Residue |
| C | GLU8 |
| C | TYR10 |
| C | VAL52 |
| C | GLN53 |
| C | TYR62 |
| C | HIS63 |
| C | ASP87 |
| C | ASP161 |
| C | SER162 |
| C | ASP164 |
| C | TYR229 |
| C | TRP233 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AG3 E1003 |
| Chain | Residue |
| E | GLU8 |
| E | TYR10 |
| E | VAL52 |
| E | GLN53 |
| E | TYR62 |
| E | HIS63 |
| E | ASP87 |
| E | ASP161 |
| E | SER162 |
| E | ASP164 |
| E | TYR229 |
| E | TRP233 |
| E | HOH1015 |
Functional Information from PROSITE/UniProt
| site_id | PS01330 |
| Number of Residues | 14 |
| Details | PABS_1 Polyamine biosynthesis (PABS) domain signature. VLIIGGGdGgaIrE |
| Chain | Residue | Details |
| A | VAL80-GLU93 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 699 |
| Details | Domain: {"description":"PABS","evidences":[{"source":"HAMAP-Rule","id":"MF_00198","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00198","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of spermidine synthase from Pyrococcus horikoshII OT3.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00198","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of spermidine synthase from Pyrococcus horikoshII OT3.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}},{"source":"PDB","id":"2E5W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00198","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of spermidine synthase from Pyrococcus horikoshII OT3.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}},{"source":"PDB","id":"2E5W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






