3PGH

CYCLOOXYGENASE-2 (PROSTAGLANDIN SYNTHASE-2) COMPLEXED WITH A NON-SELECTIVE INHIBITOR, FLURBIPROFEN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001516	biological_process	prostaglandin biosynthetic process
A	0004601	molecular_function	peroxidase activity
A	0004666	molecular_function	prostaglandin-endoperoxide synthase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005637	cellular_component	nuclear inner membrane
A	0005640	cellular_component	nuclear outer membrane
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0006693	biological_process	prostaglandin metabolic process
A	0006979	biological_process	response to oxidative stress
A	0007566	biological_process	embryo implantation
A	0008015	biological_process	blood circulation
A	0008217	biological_process	regulation of blood pressure
A	0009624	biological_process	response to nematode
A	0010269	biological_process	response to selenium ion
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0019371	biological_process	cyclooxygenase pathway
A	0019899	molecular_function	enzyme binding
A	0020037	molecular_function	heme binding
A	0030216	biological_process	keratinocyte differentiation
A	0030282	biological_process	bone mineralization
A	0031394	biological_process	positive regulation of prostaglandin biosynthetic process
A	0031622	biological_process	positive regulation of fever generation
A	0032310	biological_process	prostaglandin secretion
A	0042127	biological_process	regulation of cell population proliferation
A	0042803	molecular_function	protein homodimerization activity
A	0043005	cellular_component	neuron projection
A	0043066	biological_process	negative regulation of apoptotic process
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0046457	biological_process	prostanoid biosynthetic process
A	0046697	biological_process	decidualization
A	0046872	molecular_function	metal ion binding
A	0050873	biological_process	brown fat cell differentiation
A	0051213	molecular_function	dioxygenase activity
A	0071456	biological_process	cellular response to hypoxia
A	0071471	biological_process	cellular response to non-ionic osmotic stress
A	0071498	biological_process	cellular response to fluid shear stress
A	0090336	biological_process	positive regulation of brown fat cell differentiation
A	0098869	biological_process	cellular oxidant detoxification
A	0150077	biological_process	regulation of neuroinflammatory response
A	1902219	biological_process	negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress
B	0001516	biological_process	prostaglandin biosynthetic process
B	0004601	molecular_function	peroxidase activity
B	0004666	molecular_function	prostaglandin-endoperoxide synthase activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005637	cellular_component	nuclear inner membrane
B	0005640	cellular_component	nuclear outer membrane
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005829	cellular_component	cytosol
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0006693	biological_process	prostaglandin metabolic process
B	0006979	biological_process	response to oxidative stress
B	0007566	biological_process	embryo implantation
B	0008015	biological_process	blood circulation
B	0008217	biological_process	regulation of blood pressure
B	0009624	biological_process	response to nematode
B	0010269	biological_process	response to selenium ion
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0019371	biological_process	cyclooxygenase pathway
B	0019899	molecular_function	enzyme binding
B	0020037	molecular_function	heme binding
B	0030216	biological_process	keratinocyte differentiation
B	0030282	biological_process	bone mineralization
B	0031394	biological_process	positive regulation of prostaglandin biosynthetic process
B	0031622	biological_process	positive regulation of fever generation
B	0032310	biological_process	prostaglandin secretion
B	0042127	biological_process	regulation of cell population proliferation
B	0042803	molecular_function	protein homodimerization activity
B	0043005	cellular_component	neuron projection
B	0043066	biological_process	negative regulation of apoptotic process
B	0043231	cellular_component	intracellular membrane-bounded organelle
B	0046457	biological_process	prostanoid biosynthetic process
B	0046697	biological_process	decidualization
B	0046872	molecular_function	metal ion binding
B	0050873	biological_process	brown fat cell differentiation
B	0051213	molecular_function	dioxygenase activity
B	0071456	biological_process	cellular response to hypoxia
B	0071471	biological_process	cellular response to non-ionic osmotic stress
B	0071498	biological_process	cellular response to fluid shear stress
B	0090336	biological_process	positive regulation of brown fat cell differentiation
B	0098869	biological_process	cellular oxidant detoxification
B	0150077	biological_process	regulation of neuroinflammatory response
B	1902219	biological_process	negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress
C	0001516	biological_process	prostaglandin biosynthetic process
C	0004601	molecular_function	peroxidase activity
C	0004666	molecular_function	prostaglandin-endoperoxide synthase activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005637	cellular_component	nuclear inner membrane
C	0005640	cellular_component	nuclear outer membrane
C	0005737	cellular_component	cytoplasm
C	0005783	cellular_component	endoplasmic reticulum
C	0005788	cellular_component	endoplasmic reticulum lumen
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0005829	cellular_component	cytosol
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006633	biological_process	fatty acid biosynthetic process
C	0006693	biological_process	prostaglandin metabolic process
C	0006979	biological_process	response to oxidative stress
C	0007566	biological_process	embryo implantation
C	0008015	biological_process	blood circulation
C	0008217	biological_process	regulation of blood pressure
C	0009624	biological_process	response to nematode
C	0010269	biological_process	response to selenium ion
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
C	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C	0019371	biological_process	cyclooxygenase pathway
C	0019899	molecular_function	enzyme binding
C	0020037	molecular_function	heme binding
C	0030216	biological_process	keratinocyte differentiation
C	0030282	biological_process	bone mineralization
C	0031394	biological_process	positive regulation of prostaglandin biosynthetic process
C	0031622	biological_process	positive regulation of fever generation
C	0032310	biological_process	prostaglandin secretion
C	0042127	biological_process	regulation of cell population proliferation
C	0042803	molecular_function	protein homodimerization activity
C	0043005	cellular_component	neuron projection
C	0043066	biological_process	negative regulation of apoptotic process
C	0043231	cellular_component	intracellular membrane-bounded organelle
C	0046457	biological_process	prostanoid biosynthetic process
C	0046697	biological_process	decidualization
C	0046872	molecular_function	metal ion binding
C	0050873	biological_process	brown fat cell differentiation
C	0051213	molecular_function	dioxygenase activity
C	0071456	biological_process	cellular response to hypoxia
C	0071471	biological_process	cellular response to non-ionic osmotic stress
C	0071498	biological_process	cellular response to fluid shear stress
C	0090336	biological_process	positive regulation of brown fat cell differentiation
C	0098869	biological_process	cellular oxidant detoxification
C	0150077	biological_process	regulation of neuroinflammatory response
C	1902219	biological_process	negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress
D	0001516	biological_process	prostaglandin biosynthetic process
D	0004601	molecular_function	peroxidase activity
D	0004666	molecular_function	prostaglandin-endoperoxide synthase activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005637	cellular_component	nuclear inner membrane
D	0005640	cellular_component	nuclear outer membrane
D	0005737	cellular_component	cytoplasm
D	0005783	cellular_component	endoplasmic reticulum
D	0005788	cellular_component	endoplasmic reticulum lumen
D	0005789	cellular_component	endoplasmic reticulum membrane
D	0005829	cellular_component	cytosol
D	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006633	biological_process	fatty acid biosynthetic process
D	0006693	biological_process	prostaglandin metabolic process
D	0006979	biological_process	response to oxidative stress
D	0007566	biological_process	embryo implantation
D	0008015	biological_process	blood circulation
D	0008217	biological_process	regulation of blood pressure
D	0009624	biological_process	response to nematode
D	0010269	biological_process	response to selenium ion
D	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
D	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D	0019371	biological_process	cyclooxygenase pathway
D	0019899	molecular_function	enzyme binding
D	0020037	molecular_function	heme binding
D	0030216	biological_process	keratinocyte differentiation
D	0030282	biological_process	bone mineralization
D	0031394	biological_process	positive regulation of prostaglandin biosynthetic process
D	0031622	biological_process	positive regulation of fever generation
D	0032310	biological_process	prostaglandin secretion
D	0042127	biological_process	regulation of cell population proliferation
D	0042803	molecular_function	protein homodimerization activity
D	0043005	cellular_component	neuron projection
D	0043066	biological_process	negative regulation of apoptotic process
D	0043231	cellular_component	intracellular membrane-bounded organelle
D	0046457	biological_process	prostanoid biosynthetic process
D	0046697	biological_process	decidualization
D	0046872	molecular_function	metal ion binding
D	0050873	biological_process	brown fat cell differentiation
D	0051213	molecular_function	dioxygenase activity
D	0071456	biological_process	cellular response to hypoxia
D	0071471	biological_process	cellular response to non-ionic osmotic stress
D	0071498	biological_process	cellular response to fluid shear stress
D	0090336	biological_process	positive regulation of brown fat cell differentiation
D	0098869	biological_process	cellular oxidant detoxification
D	0150077	biological_process	regulation of neuroinflammatory response
D	1902219	biological_process	negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress

Functional Information from PDB Data

site_id	ACE
Number of Residues	1
Details	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).

Chain	Residue
A	SER530

---

site_id	CAT
Number of Residues	1
Details	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.

Chain	Residue
A	TYR385

---

site_id	HEM
Number of Residues	1
Details	HIS 388 IS THE AXIAL LIGAND TO THE HEME.

Chain	Residue
A	HIS388

---

site_id	SUB
Number of Residues	1
Details	ARGININE 120 IS BELIEVED TO ANCHOR THE CARBOXYLATE OF THE SUBSTRATE BY FORMING AN ION-PAIR.

Chain	Residue
A	ARG120

---

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	HIS207
C	HIS207
D	HIS207

---

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	TYR385
C	TYR385
D	TYR385

---

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	ARG120
B	TYR355
C	ARG120
C	TYR355
D	ARG120
D	TYR355

---

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	HIS388
C	HIS388
D	HIS388

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Aspirin-acetylated serine

Chain	Residue	Details
A	SER530
B	SER530
C	SER530
D	SER530

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	SITE: Not glycosylated => ECO:0000269|PubMed:8349699

Chain	Residue	Details
A	ASN606
B	ASN606
C	ASN606
D	ASN606

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P35354

Chain	Residue	Details
A	CYS540
B	CYS540
C	CYS540
D	CYS540

---

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	SER579
C	SER579
D	SER579

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	CARBOHYD: 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

Chain	Residue	Details
A	ASN68
B	ASN68
C	ASN68
D	ASN68

---

site_id	SWS_FT_FI10
Number of Residues	4
Details	CARBOHYD: 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

Chain	Residue	Details
A	ASN144
B	ASN144
C	ASN144
D	ASN144

---

site_id	SWS_FT_FI11
Number of Residues	4
Details	CARBOHYD: 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

Chain	Residue	Details
A	ASN410
B	ASN410
C	ASN410
D	ASN410

---

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	ASN594
C	ASN594
D	ASN594

---

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	VAL291

---

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1mhl

Chain	Residue	Details
C	VAL291

---

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1mhl

Chain	Residue	Details
D	VAL291

---

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	HIS207
B	TYR385
B	GLN203

---

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1mhl

Chain	Residue	Details
C	HIS207
C	TYR385
C	GLN203

---

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1mhl

Chain	Residue	Details
D	HIS207
D	TYR385
D	GLN203

---

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	GLN203	electrostatic stabiliser, hydrogen bond donor
B	HIS207	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	LEU384	steric role
B	TYR385	hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, radical stabiliser
B	HIS388	metal ligand
B	GLY526	steric role
B	SER530	electrostatic stabiliser

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site_id	MCSA3
Number of Residues	7
Details	M-CSA 37

Chain	Residue	Details
C	GLN203	electrostatic stabiliser, hydrogen bond donor
C	HIS207	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	LEU384	steric role
C	TYR385	hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, radical stabiliser
C	HIS388	metal ligand
C	GLY526	steric role
C	SER530	electrostatic stabiliser

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site_id	MCSA4
Number of Residues	7
Details	M-CSA 37

Chain	Residue	Details
D	GLN203	electrostatic stabiliser, hydrogen bond donor
D	HIS207	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	LEU384	steric role
D	TYR385	hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, radical stabiliser
D	HIS388	metal ligand
D	GLY526	steric role
D	SER530	electrostatic stabiliser

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