1PXX
CRYSTAL STRUCTURE OF DICLOFENAC BOUND TO THE CYCLOOXYGENASE ACTIVE SITE OF COX-2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0020037 | molecular_function | heme binding |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0020037 | molecular_function | heme binding |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0020037 | molecular_function | heme binding |
| D | 0004601 | molecular_function | peroxidase activity |
| D | 0006979 | biological_process | response to oxidative stress |
| D | 0020037 | molecular_function | heme binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:20463020 |
| Chain | Residue | Details |
| A | HIS207 | |
| B | HIS1207 | |
| C | HIS2207 | |
| D | HIS3207 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: For cyclooxygenase activity => ECO:0000269|PubMed:20463020 |
| Chain | Residue | Details |
| A | TYR385 | |
| B | TYR1385 | |
| C | TYR2385 | |
| D | TYR3385 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK |
| Chain | Residue | Details |
| A | ARG120 | |
| A | TYR355 | |
| B | ARG1120 | |
| B | TYR1355 | |
| C | ARG2120 | |
| C | TYR2355 | |
| D | ARG3120 | |
| D | TYR3355 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:5COX, ECO:0007744|PDB:6COX |
| Chain | Residue | Details |
| A | HIS388 | |
| B | HIS1388 | |
| C | HIS2388 | |
| D | HIS3388 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Aspirin-acetylated serine |
| Chain | Residue | Details |
| A | SER530 | |
| B | SER1530 | |
| C | SER2530 | |
| D | SER3530 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | SITE: Not glycosylated => ECO:0000269|PubMed:8349699 |
| Chain | Residue | Details |
| A | ASN606 | |
| B | ASN1606 | |
| C | ASN2606 | |
| D | ASN3606 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P35354 |
| Chain | Residue | Details |
| A | CYS540 | |
| B | CYS1540 | |
| C | CYS2540 | |
| D | CYS3540 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: O-acetylserine; by SPHK1 => ECO:0000269|PubMed:29662056 |
| Chain | Residue | Details |
| A | SER579 | |
| B | SER1579 | |
| C | SER2579 | |
| D | SER3579 |
| Chain | Residue | Details |
| A | ASN68 | |
| B | ASN1068 | |
| C | ASN2068 | |
| D | ASN3068 |
| Chain | Residue | Details |
| A | ASN144 | |
| B | ASN1144 | |
| C | ASN2144 | |
| D | ASN3144 |
| Chain | Residue | Details |
| A | ASN410 | |
| B | ASN1410 | |
| C | ASN2410 | |
| D | ASN3410 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:8349699 |
| Chain | Residue | Details |
| A | ASN594 | |
| B | ASN1594 | |
| C | ASN2594 | |
| D | ASN3594 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| A | VAL291 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| B | VAL1291 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| C | VAL2291 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| D | VAL3291 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| A | HIS207 | |
| A | TYR385 | |
| A | GLN203 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| B | TYR1385 | |
| B | GLN1203 | |
| B | HIS1207 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| C | TYR2385 | |
| C | HIS2207 | |
| C | GLN2203 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| D | TYR3385 | |
| D | HIS3207 | |
| D | GLN3203 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 37 |
| Chain | Residue | Details |
| A | GLN203 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS207 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LEU384 | steric role |
| A | TYR385 | hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, radical stabiliser |
| A | HIS388 | metal ligand |
| A | GLY526 | steric role |
| A | SER530 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 37 |
| Chain | Residue | Details |
| B | GLN1203 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS1207 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | LEU1384 | steric role |
| B | TYR1385 | hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, radical stabiliser |
| B | HIS1388 | metal ligand |
| B | GLY1526 | steric role |
| B | SER1530 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 37 |
| Chain | Residue | Details |
| C | GLN2203 | electrostatic stabiliser, hydrogen bond donor |
| C | HIS2207 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | LEU2384 | steric role |
| C | TYR2385 | hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, radical stabiliser |
| C | HIS2388 | metal ligand |
| C | GLY2526 | steric role |
| C | SER2530 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 7 |
| Details | M-CSA 37 |
| Chain | Residue | Details |
| D | GLN3203 | electrostatic stabiliser, hydrogen bond donor |
| D | HIS3207 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | LEU3384 | steric role |
| D | TYR3385 | hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, radical stabiliser |
| D | HIS3388 | metal ligand |
| D | GLY3526 | steric role |
| D | SER3530 | electrostatic stabiliser |
