3GZD
Human selenocysteine lyase, P1 crystal form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0009000 | molecular_function | selenocysteine lyase activity |
| A | 0016261 | biological_process | selenocysteine catabolic process |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0070279 | molecular_function | vitamin B6 binding |
| A | 1902494 | cellular_component | catalytic complex |
| B | 0005515 | molecular_function | protein binding |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0005829 | cellular_component | cytosol |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0009000 | molecular_function | selenocysteine lyase activity |
| B | 0016261 | biological_process | selenocysteine catabolic process |
| B | 0016597 | molecular_function | amino acid binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0070279 | molecular_function | vitamin B6 binding |
| B | 1902494 | cellular_component | catalytic complex |
| C | 0005515 | molecular_function | protein binding |
| C | 0005794 | cellular_component | Golgi apparatus |
| C | 0005829 | cellular_component | cytosol |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0009000 | molecular_function | selenocysteine lyase activity |
| C | 0016261 | biological_process | selenocysteine catabolic process |
| C | 0016597 | molecular_function | amino acid binding |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0070279 | molecular_function | vitamin B6 binding |
| C | 1902494 | cellular_component | catalytic complex |
| D | 0005515 | molecular_function | protein binding |
| D | 0005794 | cellular_component | Golgi apparatus |
| D | 0005829 | cellular_component | cytosol |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0009000 | molecular_function | selenocysteine lyase activity |
| D | 0016261 | biological_process | selenocysteine catabolic process |
| D | 0016597 | molecular_function | amino acid binding |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0070279 | molecular_function | vitamin B6 binding |
| D | 1902494 | cellular_component | catalytic complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLR A 500 |
| Chain | Residue |
| A | GLY99 |
| A | HIS258 |
| A | LYS259 |
| A | HOH457 |
| A | HOH462 |
| A | HOH504 |
| A | NO3600 |
| B | THR296 |
| A | THR100 |
| A | HIS145 |
| A | MET194 |
| A | ASN198 |
| A | ASP233 |
| A | ALA235 |
| A | GLN236 |
| A | VAL256 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NO3 A 600 |
| Chain | Residue |
| A | ASN37 |
| A | ALA38 |
| A | ASN198 |
| A | LYS259 |
| A | ALA386 |
| A | ALA387 |
| A | CSS388 |
| A | ARG415 |
| A | PLR500 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLR B 500 |
| Chain | Residue |
| A | GLY295 |
| A | THR296 |
| B | GLY99 |
| B | THR100 |
| B | HIS145 |
| B | MET194 |
| B | ASP233 |
| B | ALA235 |
| B | GLN236 |
| B | VAL256 |
| B | HIS258 |
| B | LYS259 |
| B | HOH452 |
| B | HOH473 |
| B | HOH497 |
| B | NO3600 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NO3 B 600 |
| Chain | Residue |
| B | ASN37 |
| B | ALA38 |
| B | ASN198 |
| B | LYS259 |
| B | ARG415 |
| B | PLR500 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLR C 500 |
| Chain | Residue |
| C | GLY99 |
| C | THR100 |
| C | HIS145 |
| C | MET194 |
| C | ASP233 |
| C | ALA235 |
| C | GLN236 |
| C | VAL256 |
| C | HIS258 |
| C | LYS259 |
| C | HOH476 |
| C | HOH486 |
| C | HOH592 |
| C | NO3600 |
| D | THR296 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 C 600 |
| Chain | Residue |
| C | ASN37 |
| C | ALA38 |
| C | ASN198 |
| C | ALA386 |
| C | ALA387 |
| C | ARG415 |
| C | PLR500 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLR D 500 |
| Chain | Residue |
| C | THR296 |
| D | GLY99 |
| D | THR100 |
| D | HIS145 |
| D | MET194 |
| D | ASP233 |
| D | ALA235 |
| D | GLN236 |
| D | VAL256 |
| D | HIS258 |
| D | LYS259 |
| D | HOH461 |
| D | HOH468 |
| D | HOH499 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 D 600 |
| Chain | Residue |
| D | ASN37 |
| D | ALA38 |
| D | ASN198 |
| D | ALA386 |
| D | ALA387 |
| D | CSS388 |
| D | ARG415 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"S-selanylcysteine intermediate","evidences":[{"source":"UniProtKB","id":"Q68FT9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2006","submissionDatabase":"PDB data bank","title":"Structure of human selenocysteine lyase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | PHE138 | |
| A | ASP233 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | LYS259 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| D | LYS259 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| C | CYS388 | |
| C | LYS259 |
| site_id | CSA13 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | ARG69 |
| site_id | CSA14 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | ARG69 |
| site_id | CSA15 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| D | ARG69 |
| site_id | CSA16 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| C | ARG69 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | PHE138 | |
| B | ASP233 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| D | PHE138 | |
| D | ASP233 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| C | PHE138 | |
| C | ASP233 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | LYS259 | |
| A | HIS145 | |
| A | ASP233 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | LYS259 | |
| B | HIS145 | |
| B | ASP233 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| D | LYS259 | |
| D | HIS145 | |
| D | ASP233 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| C | LYS259 | |
| C | HIS145 | |
| C | ASP233 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | LYS259 |
