eF-site ID 5ikr-B
PDB Code 5ikr
Chain B

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Title The Structure of Mefenamic Acid Bound to Human Cyclooxygenase-2
Classification OXIDOREDUCTASE
Compound Prostaglandin G/H synthase 2
Source (PGH2_HUMAN)
Sequence B:  NPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCSTPE
FLTRIKLFLKPTPNTVHYILTHFKGFWNVVNNIPFLRNAI
MSYVLTSRSHLIDSPPTYNADYGYKSWEAFSNLSYYTRAL
PPVPDDCPTPLGVKGKKQLPDSNEIVEKLLLRRKFIPDPQ
GSNMMFAFFAQHFTHQFFKTDHKRGPAFTNGLGHGVDLNH
IYGETLARQRKLRLFKDGKMKYQIIDGEMYPPTVKDTQAE
MIYPPQVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRV
CDVLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHL
SGYHFKLKFDPELLFNKQFQYQNRIAAEFNTLYHWHPLLP
DTFQIHDQKYNYQQFIYNNSILLEHGITQFVESFTRQIAG
RVAGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFML
KPYESFEELTGEKEMSAELEALYGDIDAVELYPALLVEKP
RPDAIFGETMVEVGAPFSLKGLMGNVICSPAYWKPSTFGG
EVGFQIINTASIQSLICNNVKGCPFTSFSVP
Description (1)  Prostaglandin G/H synthase 2 (E.C.1.14.99.1)


Functional site

1) chain B
residue 144
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593, ECO:0000269|PubMed:27710942, ECO:0007744|PDB:5F19, ECO:0007744|PDB:5F1A, ECO:0007744|PDB:5IKQ, ECO:0007744|PDB:5IKR, ECO:0007744|PDB:5IKT, ECO:0007744|PDB:5IKV, ECO:0007744|PDB:5KIR
source Swiss-Prot : SWS_FT_FI9

2) chain B
residue 410
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593, ECO:0000269|PubMed:27710942, ECO:0007744|PDB:5F19, ECO:0007744|PDB:5F1A, ECO:0007744|PDB:5IKQ, ECO:0007744|PDB:5IKR, ECO:0007744|PDB:5IKT, ECO:0007744|PDB:5IKV, ECO:0007744|PDB:5KIR
source Swiss-Prot : SWS_FT_FI9

3) chain B
residue 530
type SITE
sequence S
description Aspirin-acetylated serine => ECO:0000269|PubMed:26859324
source Swiss-Prot : SWS_FT_FI5

4) chain B
residue 540
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000305|PubMed:16373578
source Swiss-Prot : SWS_FT_FI6

5) chain B
residue 579
type MOD_RES
sequence S
description O-acetylserine => ECO:0000250|UniProtKB:Q05769
source Swiss-Prot : SWS_FT_FI7

6) chain B
residue 68
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593, ECO:0007744|PDB:5F19, ECO:0007744|PDB:5F1A, ECO:0007744|PDB:5IKQ, ECO:0007744|PDB:5IKT
source Swiss-Prot : SWS_FT_FI8

7) chain B
residue 388
type BINDING
sequence H
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00298
source Swiss-Prot : SWS_FT_FI4

8) chain B
residue 207
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298
source Swiss-Prot : SWS_FT_FI1

9) chain B
residue 385
type ACT_SITE
sequence Y
description For cyclooxygenase activity => ECO:0000250|UniProtKB:Q05769
source Swiss-Prot : SWS_FT_FI2

10) chain B
residue 120
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:Q05769
source Swiss-Prot : SWS_FT_FI3

11) chain B
residue 355
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:Q05769
source Swiss-Prot : SWS_FT_FI3


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