6VND
Quaternary Complex of human dihydroorotate dehydrogenase (DHODH) with flavin mononucleotide (FMN), orotic acid and AG-636
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004151 | molecular_function | dihydroorotase activity |
A | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0005829 | cellular_component | cytosol |
A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
A | 0006225 | biological_process | UDP biosynthetic process |
A | 0009220 | biological_process | pyrimidine ribonucleotide biosynthetic process |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
A | 0106430 | molecular_function | dihydroorotate dehydrogenase (quinone) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue R4P A 401 |
Chain | Residue |
A | TYR37 |
A | LEU66 |
A | LEU67 |
A | ARG135 |
A | TYR355 |
A | THR359 |
A | PRO363 |
A | DDQ404 |
A | HOH573 |
A | LEU41 |
A | MET42 |
A | GLN46 |
A | PRO51 |
A | ALA54 |
A | HIS55 |
A | ALA58 |
A | THR62 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue DET A 402 |
Chain | Residue |
A | ARG56 |
A | LYS99 |
A | HIS100 |
A | PRO124 |
A | GLN125 |
A | GLU126 |
A | ASN149 |
A | SER150 |
A | HIS151 |
A | NA407 |
A | HOH613 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue DET A 403 |
Chain | Residue |
A | GLU138 |
A | ASP139 |
A | GLN140 |
A | PRO289 |
A | LYS306 |
A | PRO307 |
A | ASP310 |
A | GLN314 |
A | ARG317 |
A | ASP392 |
A | HOH528 |
A | HOH542 |
A | HOH545 |
A | HOH611 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue DDQ A 404 |
Chain | Residue |
A | LEU57 |
A | PHE61 |
A | LEU67 |
A | PRO68 |
A | R4P401 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue DDQ A 405 |
Chain | Residue |
A | GLN140 |
A | ARG346 |
A | TRP361 |
A | GLN380 |
A | PHE382 |
A | ALA391 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue CL A 406 |
Chain | Residue |
A | ARG297 |
A | SER298 |
A | HOH521 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue NA A 407 |
Chain | Residue |
A | GLU52 |
A | ARG56 |
A | DET402 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue NA A 408 |
Chain | Residue |
A | ARG161 |
A | GLU265 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue NA A 409 |
Chain | Residue |
A | LYS226 |
A | ARG230 |
A | SER269 |
A | GLU273 |
site_id | AD1 |
Number of Residues | 26 |
Details | binding site for residue FMN A 410 |
Chain | Residue |
A | ALA94 |
A | ALA95 |
A | GLY96 |
A | LYS99 |
A | GLY118 |
A | SER119 |
A | ASN144 |
A | TYR146 |
A | ASN180 |
A | ASN211 |
A | LYS254 |
A | THR282 |
A | ASN283 |
A | THR284 |
A | SER304 |
A | GLY305 |
A | LEU308 |
A | VAL332 |
A | GLY333 |
A | GLY334 |
A | LEU354 |
A | TYR355 |
A | THR356 |
A | ORO411 |
A | HOH514 |
A | HOH539 |
site_id | AD2 |
Number of Residues | 11 |
Details | binding site for residue ORO A 411 |
Chain | Residue |
A | ASN283 |
A | THR284 |
A | FMN410 |
A | LYS99 |
A | ASN144 |
A | TYR146 |
A | GLY147 |
A | PHE148 |
A | ASN211 |
A | SER214 |
A | ASN216 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue ACT A 412 |
Chain | Residue |
A | THR260 |
A | GLN262 |
A | HOH634 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue ACT A 413 |
Chain | Residue |
A | ALA162 |
A | LYS166 |
A | LYS226 |
A | GLU265 |
A | ASP266 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue ACT A 414 |
Chain | Residue |
A | ARG248 |
A | HOH561 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue GOL A 415 |
Chain | Residue |
A | ASP105 |
A | TYR108 |
A | HOH546 |
A | HOH633 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue GOL A 416 |
Chain | Residue |
A | PRO129 |
A | ARG130 |
A | PRO131 |
A | ARG145 |
A | GLN238 |
site_id | AD8 |
Number of Residues | 8 |
Details | binding site for residue GOL A 417 |
Chain | Residue |
A | GLN164 |
A | GLN167 |
A | ALA168 |
A | THR171 |
A | LEU204 |
A | ASP206 |
A | HOH506 |
A | HOH525 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue GOL A 418 |
Chain | Residue |
A | ARG56 |
A | LEU57 |
A | HOH568 |
A | HOH640 |
site_id | AE1 |
Number of Residues | 6 |
Details | binding site for residue GOL A 419 |
Chain | Residue |
A | TYR320 |
A | ALA321 |
A | HIS393 |
A | HOH505 |
A | HOH543 |
A | HOH550 |
site_id | AE2 |
Number of Residues | 2 |
Details | binding site for residue GOL A 420 |
Chain | Residue |
A | GLY47 |
A | LEU48 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 364 |
Details | TOPO_DOM: Mitochondrial intermembrane => ECO:0000250 |
Chain | Residue | Details |
A | THR31-ARG395 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | SER214 |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261 |
Chain | Residue | Details |
A | ALA95 | |
A | SER119 | |
A | ASN180 | |
A | ASN211 | |
A | LYS254 | |
A | THR282 | |
A | GLY305 | |
A | GLY334 | |
A | TYR355 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS99 | |
A | ASN144 | |
A | ASN283 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 109 |
Chain | Residue | Details |
A | ASN144 | electrostatic stabiliser |
A | PHE148 | activator, electrostatic stabiliser, enhance reactivity, polar/non-polar interaction |
A | SER214 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar/non-polar interaction, proton acceptor, proton donor, proton relay |
A | ASN216 | electrostatic stabiliser |
A | THR217 | activator, electrostatic stabiliser, enhance reactivity, hydrogen bond acceptor |
A | LYS254 | electrostatic stabiliser, hydrogen bond donor |
A | ASN283 | electrostatic stabiliser |