7MMR
Crystal Structure of the Class Ie Ribonucleotide Reductase Beta-NrdI complex from Aerococcus urinae in Oxidized Form with Cu(I) bound
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
A | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
B | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
C | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
C | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
C | 0016020 | cellular_component | membrane |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
D | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
D | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
D | 0016020 | cellular_component | membrane |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0046872 | molecular_function | metal ion binding |
E | 0000166 | molecular_function | nucleotide binding |
E | 0010181 | molecular_function | FMN binding |
E | 0036211 | biological_process | protein modification process |
F | 0000166 | molecular_function | nucleotide binding |
F | 0010181 | molecular_function | FMN binding |
F | 0036211 | biological_process | protein modification process |
G | 0000166 | molecular_function | nucleotide binding |
G | 0010181 | molecular_function | FMN binding |
G | 0036211 | biological_process | protein modification process |
H | 0000166 | molecular_function | nucleotide binding |
H | 0010181 | molecular_function | FMN binding |
H | 0036211 | biological_process | protein modification process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue CU1 A 401 |
Chain | Residue |
A | VAL116 |
A | PRO176 |
A | HIS213 |
A | HOH553 |
A | HOH597 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue CU1 A 402 |
Chain | Residue |
A | THR75 |
A | CYS131 |
A | GLN135 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | ASN42 |
A | ARG43 |
E | TYR50 |
E | GLY52 |
E | FMN201 |
A | GLU39 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue CU1 B 401 |
Chain | Residue |
B | VAL116 |
B | PRO176 |
B | HIS213 |
B | HOH550 |
B | HOH586 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue CU1 B 402 |
Chain | Residue |
B | THR75 |
B | CYS131 |
B | GLN135 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
B | TYR6 |
B | SER11 |
B | ARG25 |
B | SER100 |
B | LEU101 |
B | GLN106 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue GOL B 404 |
Chain | Residue |
B | TRP63 |
B | ASN64 |
B | GLN71 |
B | LEU130 |
B | CYS131 |
B | GLN135 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue CU1 C 401 |
Chain | Residue |
C | VAL116 |
C | HIS213 |
C | HOH571 |
C | HOH594 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue CU1 C 402 |
Chain | Residue |
C | HIS256 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue GOL C 403 |
Chain | Residue |
C | TYR6 |
C | SER11 |
C | ARG25 |
C | SER100 |
C | LEU101 |
C | GLN106 |
C | HOH504 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue TRS C 404 |
Chain | Residue |
C | TRP63 |
C | ASN64 |
C | GLN71 |
C | LEU130 |
C | THR132 |
C | GLN135 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue CU1 C 405 |
Chain | Residue |
C | TRP63 |
C | THR75 |
C | CYS131 |
C | GLN135 |
site_id | AD4 |
Number of Residues | 1 |
Details | binding site for residue CA C 406 |
Chain | Residue |
C | GLU299 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue CA C 407 |
Chain | Residue |
C | GLY263 |
C | ASP266 |
C | GLU267 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue CA C 408 |
Chain | Residue |
C | GLU52 |
C | ARG121 |
D | TRP41 |
D | HOH546 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue CU1 D 401 |
Chain | Residue |
D | VAL116 |
D | PRO176 |
D | HIS213 |
D | HOH563 |
D | HOH597 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue CU1 D 402 |
Chain | Residue |
D | THR75 |
D | CYS131 |
D | GLN135 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue GOL D 403 |
Chain | Residue |
D | TYR6 |
D | SER11 |
D | GLU14 |
D | ARG25 |
D | LEU101 |
D | GLU103 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue GOL D 404 |
Chain | Residue |
D | TRP63 |
D | ASN64 |
D | GLN71 |
D | LEU130 |
D | GLN135 |
site_id | AE2 |
Number of Residues | 23 |
Details | binding site for residue FMN E 201 |
Chain | Residue |
E | PHE95 |
E | SER98 |
E | PHE99 |
E | ALA100 |
E | LEU120 |
E | CA202 |
E | HOH307 |
A | PHE215 |
A | GOL403 |
E | SER9 |
E | THR10 |
E | SER12 |
E | ASN13 |
E | ASN14 |
E | THR15 |
E | PRO48 |
E | THR49 |
E | TYR50 |
E | SER51 |
E | GLY52 |
E | GLY53 |
E | GLY91 |
E | ASN92 |
site_id | AE3 |
Number of Residues | 4 |
Details | binding site for residue CA E 202 |
Chain | Residue |
A | ASN282 |
E | ASN92 |
E | LEU120 |
E | FMN201 |
site_id | AE4 |
Number of Residues | 22 |
Details | binding site for residue FMN G 201 |
Chain | Residue |
C | PHE215 |
G | SER9 |
G | THR10 |
G | SER12 |
G | ASN13 |
G | ASN14 |
G | THR15 |
G | PRO48 |
G | THR49 |
G | TYR50 |
G | SER51 |
G | GLY52 |
G | GLY53 |
G | GLY91 |
G | ASN92 |
G | PHE95 |
G | SER98 |
G | PHE99 |
G | ALA100 |
G | LEU120 |
G | CA202 |
G | HOH310 |
site_id | AE5 |
Number of Residues | 4 |
Details | binding site for residue CA G 202 |
Chain | Residue |
C | ASN282 |
G | ASN92 |
G | LEU120 |
G | FMN201 |
site_id | AE6 |
Number of Residues | 23 |
Details | binding site for residue FMN F 201 |
Chain | Residue |
B | GLU39 |
B | PHE215 |
F | SER9 |
F | THR10 |
F | SER12 |
F | ASN13 |
F | ASN14 |
F | THR15 |
F | PRO48 |
F | THR49 |
F | TYR50 |
F | SER51 |
F | GLY52 |
F | GLY53 |
F | GLY91 |
F | ASN92 |
F | PHE95 |
F | SER98 |
F | PHE99 |
F | ALA100 |
F | LEU120 |
F | CA202 |
F | HOH311 |
site_id | AE7 |
Number of Residues | 4 |
Details | binding site for residue CA F 202 |
Chain | Residue |
B | ASN282 |
F | ASN92 |
F | LEU120 |
F | FMN201 |
site_id | AE8 |
Number of Residues | 23 |
Details | binding site for residue FMN H 201 |
Chain | Residue |
D | GLU39 |
D | PHE215 |
H | SER9 |
H | THR10 |
H | SER12 |
H | ASN13 |
H | ASN14 |
H | THR15 |
H | PRO48 |
H | THR49 |
H | TYR50 |
H | SER51 |
H | GLY52 |
H | GLY53 |
H | GLY91 |
H | ASN92 |
H | PHE95 |
H | SER98 |
H | PHE99 |
H | ALA100 |
H | LEU120 |
H | CA202 |
H | HOH306 |
site_id | AE9 |
Number of Residues | 3 |
Details | binding site for residue CA H 202 |
Chain | Residue |
H | ASN92 |
H | LEU120 |
H | FMN201 |