2Z67
Crystal structure of archaeal O-phosphoseryl-tRNA(Sec) selenium transferase (SepSecS)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0001514 | biological_process | selenocysteine incorporation |
| A | 0001717 | biological_process | conversion of seryl-tRNAsec to selenocys-tRNAsec |
| A | 0003723 | molecular_function | RNA binding |
| A | 0006412 | biological_process | translation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0098621 | molecular_function | O-phosphoseryl-tRNA(Sec) selenium transferase activity |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0001514 | biological_process | selenocysteine incorporation |
| B | 0001717 | biological_process | conversion of seryl-tRNAsec to selenocys-tRNAsec |
| B | 0003723 | molecular_function | RNA binding |
| B | 0006412 | biological_process | translation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0098621 | molecular_function | O-phosphoseryl-tRNA(Sec) selenium transferase activity |
| C | 0000049 | molecular_function | tRNA binding |
| C | 0001514 | biological_process | selenocysteine incorporation |
| C | 0001717 | biological_process | conversion of seryl-tRNAsec to selenocys-tRNAsec |
| C | 0003723 | molecular_function | RNA binding |
| C | 0006412 | biological_process | translation |
| C | 0016740 | molecular_function | transferase activity |
| C | 0098621 | molecular_function | O-phosphoseryl-tRNA(Sec) selenium transferase activity |
| D | 0000049 | molecular_function | tRNA binding |
| D | 0001514 | biological_process | selenocysteine incorporation |
| D | 0001717 | biological_process | conversion of seryl-tRNAsec to selenocys-tRNAsec |
| D | 0003723 | molecular_function | RNA binding |
| D | 0006412 | biological_process | translation |
| D | 0016740 | molecular_function | transferase activity |
| D | 0098621 | molecular_function | O-phosphoseryl-tRNA(Sec) selenium transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1002 |
| Chain | Residue |
| B | ARG94 |
| B | SER95 |
| B | GLN102 |
| B | ARG307 |
| B | HOH1005 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1002 |
| Chain | Residue |
| C | ARG94 |
| C | SER95 |
| C | GLN102 |
| C | ARG307 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 1001 |
| Chain | Residue |
| A | SER138 |
| A | THR139 |
| A | GLY140 |
| A | HIS166 |
| A | SER168 |
| A | THR220 |
| A | ASN247 |
| A | ALA249 |
| A | TYR250 |
| A | LYS278 |
| B | GLU71 |
| B | ARG72 |
| B | GLY306 |
| B | ARG307 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 1001 |
| Chain | Residue |
| A | ARG72 |
| A | GLY306 |
| A | ARG307 |
| B | SER138 |
| B | THR139 |
| B | GLY140 |
| B | HIS166 |
| B | SER168 |
| B | THR220 |
| B | PHE221 |
| B | ASN247 |
| B | ALA249 |
| B | LYS278 |
| B | HOH1029 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP C 1001 |
| Chain | Residue |
| C | SER138 |
| C | THR139 |
| C | GLY140 |
| C | HIS166 |
| C | SER168 |
| C | THR220 |
| C | PHE221 |
| C | ASN247 |
| C | TYR250 |
| C | LYS278 |
| D | ARG72 |
| D | GLY306 |
| D | ARG307 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP D 1001 |
| Chain | Residue |
| C | ARG72 |
| C | GLY306 |
| C | ARG307 |
| D | SER138 |
| D | THR139 |
| D | GLY140 |
| D | HIS166 |
| D | SER168 |
| D | THR220 |
| D | PHE221 |
| D | ASN247 |
| D | ALA249 |
| D | LYS278 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18158303 |
| Chain | Residue | Details |
| A | ARG72 | |
| B | ARG307 | |
| C | ARG72 | |
| C | ARG94 | |
| C | SER95 | |
| C | GLN102 | |
| C | ARG307 | |
| D | ARG72 | |
| D | ARG94 | |
| D | SER95 | |
| D | GLN102 | |
| A | ARG94 | |
| D | ARG307 | |
| A | SER95 | |
| A | GLN102 | |
| A | ARG307 | |
| B | ARG72 | |
| B | ARG94 | |
| B | SER95 | |
| B | GLN102 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU71 | |
| B | GLU71 | |
| C | GLU71 | |
| D | GLU71 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:17142313, ECO:0000269|PubMed:18158303 |
| Chain | Residue | Details |
| A | LYS278 | |
| B | LYS278 | |
| C | LYS278 | |
| D | LYS278 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 286 |
| Chain | Residue | Details |
| A | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| A | ARG94 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| A | SER95 | electrostatic stabiliser, hydrogen bond donor |
| A | GLN102 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | HIS166 | electrostatic stabiliser, polar interaction |
| A | ALA249 | steric role, van der waals interaction |
| A | LYS278 | activator, covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| A | ARG307 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 286 |
| Chain | Residue | Details |
| B | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| B | ARG94 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| B | SER95 | electrostatic stabiliser, hydrogen bond donor |
| B | GLN102 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | HIS166 | electrostatic stabiliser, polar interaction |
| B | ALA249 | steric role, van der waals interaction |
| B | LYS278 | activator, covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| B | ARG307 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 8 |
| Details | M-CSA 286 |
| Chain | Residue | Details |
| C | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| C | ARG94 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| C | SER95 | electrostatic stabiliser, hydrogen bond donor |
| C | GLN102 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| C | HIS166 | electrostatic stabiliser, polar interaction |
| C | ALA249 | steric role, van der waals interaction |
| C | LYS278 | activator, covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| C | ARG307 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 8 |
| Details | M-CSA 286 |
| Chain | Residue | Details |
| D | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| D | ARG94 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| D | SER95 | electrostatic stabiliser, hydrogen bond donor |
| D | GLN102 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| D | HIS166 | electrostatic stabiliser, polar interaction |
| D | ALA249 | steric role, van der waals interaction |
| D | LYS278 | activator, covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| D | ARG307 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
