4YAU
Reduced CYPOR mutant - G141del/E142N
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003420 | biological_process | regulation of growth plate cartilage chondrocyte proliferation |
A | 0003958 | molecular_function | NADPH-hemoprotein reductase activity |
A | 0004128 | molecular_function | cytochrome-b5 reductase activity, acting on NAD(P)H |
A | 0005737 | cellular_component | cytoplasm |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0005829 | cellular_component | cytosol |
A | 0006809 | biological_process | nitric oxide biosynthetic process |
A | 0007584 | biological_process | response to nutrient |
A | 0008941 | molecular_function | nitric oxide dioxygenase NAD(P)H activity |
A | 0009055 | molecular_function | electron transfer activity |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0009437 | biological_process | carnitine metabolic process |
A | 0009725 | biological_process | response to hormone |
A | 0009812 | biological_process | flavonoid metabolic process |
A | 0010181 | molecular_function | FMN binding |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019395 | biological_process | fatty acid oxidation |
A | 0019899 | molecular_function | enzyme binding |
A | 0022900 | biological_process | electron transport chain |
A | 0032332 | biological_process | positive regulation of chondrocyte differentiation |
A | 0043066 | biological_process | negative regulation of apoptotic process |
A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
A | 0043602 | biological_process | nitrate catabolic process |
A | 0045542 | biological_process | positive regulation of cholesterol biosynthetic process |
A | 0045880 | biological_process | positive regulation of smoothened signaling pathway |
A | 0046210 | biological_process | nitric oxide catabolic process |
A | 0047726 | molecular_function | iron-cytochrome-c reductase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0050661 | molecular_function | NADP binding |
A | 0070988 | biological_process | demethylation |
A | 0071371 | biological_process | cellular response to gonadotropin stimulus |
A | 0071372 | biological_process | cellular response to follicle-stimulating hormone stimulus |
A | 0071375 | biological_process | cellular response to peptide hormone stimulus |
A | 0071548 | biological_process | response to dexamethasone |
A | 0090031 | biological_process | positive regulation of steroid hormone biosynthetic process |
A | 0090181 | biological_process | regulation of cholesterol metabolic process |
A | 0090346 | biological_process | cellular organofluorine metabolic process |
B | 0003420 | biological_process | regulation of growth plate cartilage chondrocyte proliferation |
B | 0003958 | molecular_function | NADPH-hemoprotein reductase activity |
B | 0004128 | molecular_function | cytochrome-b5 reductase activity, acting on NAD(P)H |
B | 0005737 | cellular_component | cytoplasm |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0005829 | cellular_component | cytosol |
B | 0006809 | biological_process | nitric oxide biosynthetic process |
B | 0007584 | biological_process | response to nutrient |
B | 0008941 | molecular_function | nitric oxide dioxygenase NAD(P)H activity |
B | 0009055 | molecular_function | electron transfer activity |
B | 0009410 | biological_process | response to xenobiotic stimulus |
B | 0009437 | biological_process | carnitine metabolic process |
B | 0009725 | biological_process | response to hormone |
B | 0009812 | biological_process | flavonoid metabolic process |
B | 0010181 | molecular_function | FMN binding |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019395 | biological_process | fatty acid oxidation |
B | 0019899 | molecular_function | enzyme binding |
B | 0022900 | biological_process | electron transport chain |
B | 0032332 | biological_process | positive regulation of chondrocyte differentiation |
B | 0043066 | biological_process | negative regulation of apoptotic process |
B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
B | 0043602 | biological_process | nitrate catabolic process |
B | 0045542 | biological_process | positive regulation of cholesterol biosynthetic process |
B | 0045880 | biological_process | positive regulation of smoothened signaling pathway |
B | 0046210 | biological_process | nitric oxide catabolic process |
B | 0047726 | molecular_function | iron-cytochrome-c reductase activity |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0050661 | molecular_function | NADP binding |
B | 0070988 | biological_process | demethylation |
B | 0071371 | biological_process | cellular response to gonadotropin stimulus |
B | 0071372 | biological_process | cellular response to follicle-stimulating hormone stimulus |
B | 0071375 | biological_process | cellular response to peptide hormone stimulus |
B | 0071548 | biological_process | response to dexamethasone |
B | 0090031 | biological_process | positive regulation of steroid hormone biosynthetic process |
B | 0090181 | biological_process | regulation of cholesterol metabolic process |
B | 0090346 | biological_process | cellular organofluorine metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | binding site for residue FMN A 701 |
Chain | Residue |
A | SER86 |
A | ASN142 |
A | GLY143 |
A | LEU173 |
A | GLY174 |
A | ASN175 |
A | TYR178 |
A | HIS180 |
A | PHE181 |
A | ASN182 |
A | ASP208 |
A | GLN87 |
A | LEU212 |
A | HOH808 |
A | HOH986 |
A | THR88 |
A | GLY89 |
A | THR90 |
A | ALA91 |
A | ALA138 |
A | THR139 |
A | TYR140 |
site_id | AC2 |
Number of Residues | 24 |
Details | binding site for residue FAD A 702 |
Chain | Residue |
A | HIS319 |
A | ARG424 |
A | ARG454 |
A | TYR455 |
A | TYR456 |
A | SER457 |
A | CYS472 |
A | ALA473 |
A | VAL474 |
A | VAL476 |
A | TYR478 |
A | GLY488 |
A | VAL489 |
A | ALA490 |
A | THR491 |
A | TRP677 |
A | HOH809 |
A | HOH827 |
A | HOH869 |
A | HOH902 |
A | HOH922 |
A | HOH930 |
A | HOH956 |
A | HOH990 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue 2AM A 703 |
Chain | Residue |
A | GLY534 |
A | CYS566 |
A | ARG567 |
A | SER596 |
A | ARG597 |
A | LYS602 |
A | TYR604 |
A | GLN606 |
A | MET636 |
A | ASP639 |
A | HOH805 |
A | HOH848 |
A | HOH968 |
A | HOH979 |
A | HOH1026 |
A | HOH1067 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue PO4 A 704 |
Chain | Residue |
A | ASN293 |
A | GLY295 |
A | THR296 |
A | GLU297 |
A | ARG298 |
A | ARG567 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue PO4 A 705 |
Chain | Residue |
A | HIS465 |
A | PRO466 |
A | ASN467 |
A | SER468 |
site_id | AC6 |
Number of Residues | 20 |
Details | binding site for residue FMN B 701 |
Chain | Residue |
B | SER86 |
B | GLN87 |
B | THR88 |
B | GLY89 |
B | THR90 |
B | ALA91 |
B | ALA138 |
B | THR139 |
B | TYR140 |
B | ASN142 |
B | GLY143 |
B | LEU173 |
B | GLY174 |
B | ASN175 |
B | TYR178 |
B | HIS180 |
B | PHE181 |
B | ASN182 |
B | ASP208 |
B | LEU212 |
site_id | AC7 |
Number of Residues | 25 |
Details | binding site for residue FAD B 702 |
Chain | Residue |
B | ALA473 |
B | VAL474 |
B | VAL476 |
B | TYR478 |
B | GLY488 |
B | VAL489 |
B | ALA490 |
B | THR491 |
B | TRP677 |
B | HOH804 |
B | HOH811 |
B | HOH814 |
B | HOH817 |
B | HOH829 |
B | HOH832 |
B | HOH849 |
B | HOH893 |
B | HOH955 |
B | HIS319 |
B | ARG424 |
B | ARG454 |
B | TYR455 |
B | TYR456 |
B | SER457 |
B | CYS472 |
site_id | AC8 |
Number of Residues | 16 |
Details | binding site for residue 2AM B 703 |
Chain | Residue |
B | CYS566 |
B | ARG567 |
B | SER596 |
B | ARG597 |
B | LYS602 |
B | TYR604 |
B | GLN606 |
B | MET636 |
B | ASP639 |
B | HOH824 |
B | HOH874 |
B | HOH925 |
B | HOH949 |
B | HOH950 |
B | HOH951 |
B | HOH1006 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue PO4 B 704 |
Chain | Residue |
B | ASN293 |
B | GLY295 |
B | THR296 |
B | GLU297 |
B | ARG298 |
B | ARG567 |
B | GLU571 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue PO4 B 705 |
Chain | Residue |
B | HIS465 |
B | PRO466 |
B | ASN467 |
B | SER468 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue PO4 B 706 |
Chain | Residue |
A | LYS130 |
A | PHE231 |
A | HOH1027 |
B | HIS299 |
B | ARG495 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8 |
Chain | Residue | Details |
A | SER86 | |
A | SER678 | |
B | SER86 | |
B | ALA138 | |
B | GLY174 | |
B | TYR455 | |
B | GLU479 | |
B | VAL489 | |
B | GLY536 | |
B | ARG597 | |
B | VAL603 | |
A | ALA138 | |
B | SER678 | |
A | GLY174 | |
A | TYR455 | |
A | GLU479 | |
A | VAL489 | |
A | GLY536 | |
A | ARG597 | |
A | VAL603 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990 |
Chain | Residue | Details |
A | ASP209 | |
B | ASP209 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990 |
Chain | Residue | Details |
A | HIS299 | |
A | VAL640 | |
B | HIS299 | |
B | VAL640 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|Ref.8 |
Chain | Residue | Details |
A | ARG425 | |
B | ARG425 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8 |
Chain | Residue | Details |
A | ALA473 | |
B | ALA473 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 117 |
Chain | Residue | Details |
A | ILE458 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser |
A | GLY631 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction |
A | VAL676 | hydrogen bond acceptor, modifies pKa |
A | SER678 | steric role |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 117 |
Chain | Residue | Details |
B | ILE458 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser |
B | GLY631 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction |
B | VAL676 | hydrogen bond acceptor, modifies pKa |
B | SER678 | steric role |