1L1L
CRYSTAL STRUCTURE OF B-12 DEPENDENT (CLASS II) RIBONUCLEOTIDE REDUCTASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
A | 0006260 | biological_process | DNA replication |
A | 0008998 | molecular_function | ribonucleoside-triphosphate reductase (thioredoxin) activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0031419 | molecular_function | cobalamin binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
B | 0006260 | biological_process | DNA replication |
B | 0008998 | molecular_function | ribonucleoside-triphosphate reductase (thioredoxin) activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0031419 | molecular_function | cobalamin binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
C | 0006260 | biological_process | DNA replication |
C | 0008998 | molecular_function | ribonucleoside-triphosphate reductase (thioredoxin) activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0031419 | molecular_function | cobalamin binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
D | 0006260 | biological_process | DNA replication |
D | 0008998 | molecular_function | ribonucleoside-triphosphate reductase (thioredoxin) activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0031419 | molecular_function | cobalamin binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | CYS408 | |
A | GLU410 | |
B | CYS408 | |
B | GLU410 | |
C | CYS408 | |
C | GLU410 | |
D | CYS408 | |
D | GLU410 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 15158709, 15450481, 16756507, 1518709 |
Chain | Residue | Details |
A | CYS408 | |
A | GLU410 | |
A | CYS119 | |
A | CYS419 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 140 |
Chain | Residue | Details |
A | CYS119 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
A | ASN406 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
A | CYS408 | hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor |
A | GLU410 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, single electron acceptor, single electron donor, single electron relay |
A | CYS419 | electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, hydrogen radical donor, nucleofuge, proton acceptor, single electron donor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 140 |
Chain | Residue | Details |
B | CYS119 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
B | ASN406 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
B | CYS408 | hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor |
B | GLU410 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, single electron acceptor, single electron donor, single electron relay |
B | CYS419 | electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, hydrogen radical donor, nucleofuge, proton acceptor, single electron donor |
site_id | MCSA3 |
Number of Residues | 5 |
Details | M-CSA 140 |
Chain | Residue | Details |
C | CYS119 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
C | ASN406 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
C | CYS408 | hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor |
C | GLU410 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, single electron acceptor, single electron donor, single electron relay |
C | CYS419 | electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, hydrogen radical donor, nucleofuge, proton acceptor, single electron donor |
site_id | MCSA4 |
Number of Residues | 5 |
Details | M-CSA 140 |
Chain | Residue | Details |
D | CYS119 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
D | ASN406 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
D | CYS408 | hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor |
D | GLU410 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, single electron acceptor, single electron donor, single electron relay |
D | CYS419 | electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, hydrogen radical donor, nucleofuge, proton acceptor, single electron donor |