eF-site ID 6cox-A
PDB Code 6cox
Chain A

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Title CYCLOOXYGENASE-2 (PROSTAGLANDIN SYNTHASE-2) COMPLEXED WITH A SELECTIVE INHIBITOR, SC-558 IN I222 SPACE GROUP
Classification OXIDOREDUCTASE
Compound CYCLOOXYGENASE-2
Source (PGH2_MOUSE)
Sequence A:  ANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTP
EFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNNIPFLRSL
IMKYVLTSRSYLIDSPPTYNVHYGYKSWEAFSNLSYYTRA
LPPVADDCPTPMGVKGNKELPDSKEVLEKVLLRREFIPDP
QGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLN
HIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQV
EMIYPPHIPENLQFAVGQEVFGLVPGLMMYATIWLREHQR
VCDILKQEHPEWGDEQLFQTSKLILIGETIKIVIEDYVQH
LSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLL
PDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIA
GRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFS
LKPYTSFEELTGEKEMAAELKALYSDIDVMELYPALLVEK
PRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFG
GEVGFKIINTASIQSLICNNVKGCPFTSFNVQ
Description


Functional site

1) chain A
residue 385
type
sequence Y
description TYR 385 IS BELIEVED TO BE THE AMINO ACID THAT ABSTRACTS A HYDROGEN ATOM FROM THE SUBSTRATE. IT IS LOCATED CLOSE TO THE HEME. A TYROSINE RADICAL IS FORMED DURING THE COURSE OF THE REACTION.
source : CAT

2) chain A
residue 530
type
sequence S
description SER 530 IS ACETYLATED BY ASPIRIN (AN ACETYL GROUP IS COVALENTLY ATTACHED TO THE PROTEIN WHEN INHIBITED WITH ASPIRIN). THE ACETYLATED SER PREVENTS THE PROPER BINDING OF THE SUBSTRATE IN THE CYCLOOXYGENASE ACTIVE SITE. IT HAS BEEN RECENTLY SHOWN, HOWEVER, THAT ACETYLATION OF CYCLOOXYGENASE-2 RESULTS IN THE FORMATION OF A DIFFERENT PRODUCT (15-HETE).
source : ACE

3) chain A
residue 388
type
sequence H
description HIS 388 IS THE AXIAL LIGAND TO THE HEME.
source : HEM

4) chain A
residue 120
type
sequence R
description ARGININE 120 IS BELIEVED TO ANCHOR THE CARBOXYLATE OF THE SUBSTRATE BY FORMING AN ION-PAIR.
source : SUB

5) chain A
residue 530
type SITE
sequence S
description Aspirin-acetylated serine
source Swiss-Prot : SWS_FT_FI5

6) chain A
residue 207
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:20463020
source Swiss-Prot : SWS_FT_FI1

7) chain A
residue 385
type ACT_SITE
sequence Y
description For cyclooxygenase activity => ECO:0000269|PubMed:20463020
source Swiss-Prot : SWS_FT_FI2

8) chain A
residue 540
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000250|UniProtKB:P35354
source Swiss-Prot : SWS_FT_FI7

9) chain A
residue 579
type MOD_RES
sequence S
description O-acetylserine; by SPHK1 => ECO:0000269|PubMed:29662056
source Swiss-Prot : SWS_FT_FI8

10) chain A
residue 68
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI9

11) chain A
residue 203
type catalytic
sequence Q
description 37
source MCSA : MCSA1

12) chain A
residue 207
type catalytic
sequence H
description 37
source MCSA : MCSA1

13) chain A
residue 384
type catalytic
sequence L
description 37
source MCSA : MCSA1

14) chain A
residue 385
type catalytic
sequence Y
description 37
source MCSA : MCSA1

15) chain A
residue 388
type catalytic
sequence H
description 37
source MCSA : MCSA1

16) chain A
residue 526
type catalytic
sequence G
description 37
source MCSA : MCSA1

17) chain A
residue 530
type catalytic
sequence S
description 37
source MCSA : MCSA1

18) chain A
residue 144
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI10

19) chain A
residue 410
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI11

20) chain A
residue 388
type BINDING
sequence H
description 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
source Swiss-Prot : SWS_FT_FI4

21) chain A
residue 120
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
source Swiss-Prot : SWS_FT_FI3

22) chain A
residue 355
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
source Swiss-Prot : SWS_FT_FI3


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