5G5H
Escherichia coli Periplasmic Aldehyde Oxidase R440H mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0005515 | molecular_function | protein binding |
B | 0009056 | biological_process | catabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0042597 | cellular_component | periplasmic space |
B | 0046872 | molecular_function | metal ion binding |
B | 0047770 | molecular_function | carboxylate reductase activity |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
B | 0071949 | molecular_function | FAD binding |
B | 0110095 | biological_process | cellular detoxification of aldehyde |
B | 1990204 | cellular_component | oxidoreductase complex |
C | 0005506 | molecular_function | iron ion binding |
C | 0005515 | molecular_function | protein binding |
C | 0006974 | biological_process | DNA damage response |
C | 0009056 | biological_process | catabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
C | 0030151 | molecular_function | molybdenum ion binding |
C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
C | 0042597 | cellular_component | periplasmic space |
C | 0046872 | molecular_function | metal ion binding |
C | 0047770 | molecular_function | carboxylate reductase activity |
C | 0110095 | biological_process | cellular detoxification of aldehyde |
C | 1990204 | cellular_component | oxidoreductase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FES A 1226 |
Chain | Residue |
A | GLN157 |
A | CYS158 |
A | GLY159 |
A | CYS161 |
A | CYS208 |
A | ARG209 |
A | CYS210 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES A 1227 |
Chain | Residue |
A | ASP100 |
A | GLY102 |
A | GLN103 |
A | CYS104 |
A | GLY105 |
A | CYS107 |
A | CYS119 |
A | GLY98 |
A | CYS99 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 1228 |
Chain | Residue |
C | ARG272 |
C | ACT1743 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 1229 |
Chain | Residue |
A | VAL184 |
A | VAL186 |
A | GLU193 |
A | THR195 |
A | GLU198 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SF4 B 1317 |
Chain | Residue |
B | CYS119 |
B | CYS129 |
B | CYS138 |
B | ALA156 |
B | CYS157 |
B | ILE158 |
site_id | AC6 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD B 1318 |
Chain | Residue |
A | GLY102 |
B | LYS26 |
B | PHE27 |
B | ALA29 |
B | GLY30 |
B | GLY31 |
B | THR32 |
B | ASN33 |
B | LEU34 |
B | GLY98 |
B | ALA99 |
B | LEU103 |
B | ALA107 |
B | THR108 |
B | ALA110 |
B | GLY111 |
B | ASN112 |
B | LEU114 |
B | GLN115 |
B | PRO162 |
B | SER163 |
B | ASP164 |
B | LEU212 |
B | ILE213 |
B | LYS230 |
B | TYR237 |
B | ALA238 |
B | PHE239 |
B | HOH2040 |
B | HOH2058 |
B | HOH2062 |
B | HOH2155 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD B 1319 |
Chain | Residue |
B | GLN249 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD B 1320 |
Chain | Residue |
B | GLN147 |
B | THR160 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 1321 |
Chain | Residue |
B | GLN147 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 1322 |
Chain | Residue |
B | ASN130 |
B | GLY135 |
B | LYS199 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 1324 |
Chain | Residue |
B | HOH2154 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CSD C 395 |
Chain | Residue |
C | VAL387 |
C | THR393 |
C | ARG394 |
C | PHE396 |
C | SER397 |
C | TYR581 |
C | GLN582 |
site_id | BC4 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE MCN C 1732 |
Chain | Residue |
C | ALA622 |
C | GLN625 |
C | LYS688 |
C | GLY689 |
C | VAL690 |
C | GLY691 |
C | GLU692 |
C | MOS1733 |
C | HOH2324 |
C | HOH2325 |
C | HOH2339 |
A | GLN157 |
A | CYS210 |
C | GLY240 |
C | GLY241 |
C | PHE242 |
C | GLY243 |
C | ARG350 |
C | ILE468 |
C | GLY469 |
C | THR470 |
C | GLY471 |
C | SER472 |
C | GLY507 |
C | GLY508 |
C | GLN509 |
C | TRP510 |
C | GLY511 |
C | ALA512 |
C | ARG615 |
C | ILE616 |
C | LEU617 |
C | ASN618 |
C | THR621 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MOS C 1733 |
Chain | Residue |
C | GLN211 |
C | GLY243 |
C | MET349 |
C | ARG350 |
C | PRO352 |
C | GLY508 |
C | GLU692 |
C | MCN1732 |
C | HOH2338 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IOD C 1734 |
Chain | Residue |
A | GLN103 |
C | ARG272 |
C | ASP655 |
site_id | BC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD C 1735 |
Chain | Residue |
C | ASN47 |
site_id | BC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL C 1738 |
Chain | Residue |
C | ARG406 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL C 1739 |
Chain | Residue |
C | ARG527 |
C | GLN542 |
site_id | CC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL C 1740 |
Chain | Residue |
A | HOH2021 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT C 1742 |
Chain | Residue |
C | ASP93 |
C | LYS94 |
C | TRP215 |
C | ASP219 |
site_id | CC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT C 1743 |
Chain | Residue |
A | LYS97 |
A | ASP100 |
A | IOD1228 |
A | HOH2041 |
C | PHE120 |
C | MET269 |
C | PRO271 |
C | HOH2050 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 1744 |
Chain | Residue |
C | TRP41 |
C | THR170 |
C | SER171 |
C | ASP497 |
C | HOH2047 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 1745 |
Chain | Residue |
C | THR315 |
C | PRO316 |
C | GLU317 |
C | THR318 |
C | ALA348 |
C | PRO352 |
site_id | CC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 1746 |
Chain | Residue |
C | LEU29 |
C | TYR237 |
C | GLN295 |
C | TYR473 |
C | VAL493 |
Functional Information from PROSITE/UniProt
site_id | PS00197 |
Number of Residues | 9 |
Details | 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CDHGQCGAC |
Chain | Residue | Details |
A | CYS99-CYS107 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:19368556 |
Chain | Residue | Details |
C | GLU692 | |
B | THR108 | |
B | CYS119 | |
B | CYS129 | |
B | CYS138 | |
B | CYS157 | |
B | ASP164 | |
B | ILE213 | |
B | LYS230 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27622978, ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H |
Chain | Residue | Details |
C | GLY241 | |
C | ILE468 | |
C | GLY511 | |
C | ARG615 | |
C | GLN625 | |
C | LYS688 |