1KYO

YEAST CYTOCHROME BC1 COMPLEX WITH BOUND SUBSTRATE CYTOCHROME C

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004222	molecular_function	metalloendopeptidase activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
A	0006627	biological_process	protein processing involved in protein targeting to mitochondrion
A	0008121	molecular_function	quinol-cytochrome-c reductase activity
A	0009060	biological_process	aerobic respiration
A	0017087	cellular_component	mitochondrial processing peptidase complex
A	0022904	biological_process	respiratory electron transport chain
A	0045275	cellular_component	respiratory chain complex III
A	0045333	biological_process	cellular respiration
A	0046872	molecular_function	metal ion binding
A	1902600	biological_process	proton transmembrane transport
B	0004222	molecular_function	metalloendopeptidase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
B	0006508	biological_process	proteolysis
B	0008121	molecular_function	quinol-cytochrome-c reductase activity
B	0009060	biological_process	aerobic respiration
B	0016020	cellular_component	membrane
B	0022904	biological_process	respiratory electron transport chain
B	0030061	cellular_component	mitochondrial crista
B	0045275	cellular_component	respiratory chain complex III
B	0045333	biological_process	cellular respiration
B	0046872	molecular_function	metal ion binding
B	1902600	biological_process	proton transmembrane transport
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
C	0008121	molecular_function	quinol-cytochrome-c reductase activity
C	0009055	molecular_function	electron transfer activity
C	0009060	biological_process	aerobic respiration
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0022904	biological_process	respiratory electron transport chain
C	0045275	cellular_component	respiratory chain complex III
C	0045333	biological_process	cellular respiration
C	0046872	molecular_function	metal ion binding
C	1902600	biological_process	proton transmembrane transport
D	0009055	molecular_function	electron transfer activity
D	0020037	molecular_function	heme binding
E	0008121	molecular_function	quinol-cytochrome-c reductase activity
E	0016020	cellular_component	membrane
E	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
G	0005739	cellular_component	mitochondrion
G	0005743	cellular_component	mitochondrial inner membrane
G	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
G	0008121	molecular_function	quinol-cytochrome-c reductase activity
G	0009060	biological_process	aerobic respiration
G	0016020	cellular_component	membrane
G	0022904	biological_process	respiratory electron transport chain
G	0034551	biological_process	mitochondrial respiratory chain complex III assembly
G	0045275	cellular_component	respiratory chain complex III
G	0045333	biological_process	cellular respiration
G	0099617	cellular_component	matrix side of mitochondrial inner membrane
G	1902600	biological_process	proton transmembrane transport
H	0005739	cellular_component	mitochondrion
H	0005743	cellular_component	mitochondrial inner membrane
H	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
H	0008121	molecular_function	quinol-cytochrome-c reductase activity
H	0009060	biological_process	aerobic respiration
H	0016020	cellular_component	membrane
H	0022904	biological_process	respiratory electron transport chain
H	0045275	cellular_component	respiratory chain complex III
H	0045333	biological_process	cellular respiration
H	1902600	biological_process	proton transmembrane transport
I	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
I	0045275	cellular_component	respiratory chain complex III
L	0004222	molecular_function	metalloendopeptidase activity
L	0005515	molecular_function	protein binding
L	0005739	cellular_component	mitochondrion
L	0005743	cellular_component	mitochondrial inner membrane
L	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
L	0006627	biological_process	protein processing involved in protein targeting to mitochondrion
L	0008121	molecular_function	quinol-cytochrome-c reductase activity
L	0009060	biological_process	aerobic respiration
L	0017087	cellular_component	mitochondrial processing peptidase complex
L	0022904	biological_process	respiratory electron transport chain
L	0045275	cellular_component	respiratory chain complex III
L	0045333	biological_process	cellular respiration
L	0046872	molecular_function	metal ion binding
L	1902600	biological_process	proton transmembrane transport
M	0004222	molecular_function	metalloendopeptidase activity
M	0005515	molecular_function	protein binding
M	0005739	cellular_component	mitochondrion
M	0005743	cellular_component	mitochondrial inner membrane
M	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
M	0006508	biological_process	proteolysis
M	0008121	molecular_function	quinol-cytochrome-c reductase activity
M	0009060	biological_process	aerobic respiration
M	0016020	cellular_component	membrane
M	0022904	biological_process	respiratory electron transport chain
M	0030061	cellular_component	mitochondrial crista
M	0045275	cellular_component	respiratory chain complex III
M	0045333	biological_process	cellular respiration
M	0046872	molecular_function	metal ion binding
M	1902600	biological_process	proton transmembrane transport
N	0005739	cellular_component	mitochondrion
N	0005743	cellular_component	mitochondrial inner membrane
N	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
N	0008121	molecular_function	quinol-cytochrome-c reductase activity
N	0009055	molecular_function	electron transfer activity
N	0009060	biological_process	aerobic respiration
N	0016020	cellular_component	membrane
N	0016491	molecular_function	oxidoreductase activity
N	0022904	biological_process	respiratory electron transport chain
N	0045275	cellular_component	respiratory chain complex III
N	0045333	biological_process	cellular respiration
N	0046872	molecular_function	metal ion binding
N	1902600	biological_process	proton transmembrane transport
O	0009055	molecular_function	electron transfer activity
O	0020037	molecular_function	heme binding
P	0008121	molecular_function	quinol-cytochrome-c reductase activity
P	0016020	cellular_component	membrane
P	0051537	molecular_function	2 iron, 2 sulfur cluster binding
Q	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
R	0005739	cellular_component	mitochondrion
R	0005743	cellular_component	mitochondrial inner membrane
R	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
R	0008121	molecular_function	quinol-cytochrome-c reductase activity
R	0009060	biological_process	aerobic respiration
R	0016020	cellular_component	membrane
R	0022904	biological_process	respiratory electron transport chain
R	0034551	biological_process	mitochondrial respiratory chain complex III assembly
R	0045275	cellular_component	respiratory chain complex III
R	0045333	biological_process	cellular respiration
R	0099617	cellular_component	matrix side of mitochondrial inner membrane
R	1902600	biological_process	proton transmembrane transport
S	0005739	cellular_component	mitochondrion
S	0005743	cellular_component	mitochondrial inner membrane
S	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
S	0008121	molecular_function	quinol-cytochrome-c reductase activity
S	0009060	biological_process	aerobic respiration
S	0016020	cellular_component	membrane
S	0022904	biological_process	respiratory electron transport chain
S	0045275	cellular_component	respiratory chain complex III
S	0045333	biological_process	cellular respiration
S	1902600	biological_process	proton transmembrane transport
T	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
T	0045275	cellular_component	respiratory chain complex III
W	0005515	molecular_function	protein binding
W	0005739	cellular_component	mitochondrion
W	0005758	cellular_component	mitochondrial intermembrane space
W	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
W	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
W	0009055	molecular_function	electron transfer activity
W	0020037	molecular_function	heme binding
W	0022904	biological_process	respiratory electron transport chain
W	0046872	molecular_function	metal ion binding
W	1901612	molecular_function	cardiolipin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEC C 501

Chain	Residue
C	GLN43
C	ALA128
C	GLY131
C	TYR132
C	VAL135
C	HIS183
C	TYR184
C	PRO187
C	GLY47
C	ILE48
C	MET50
C	ALA51
C	ARG79
C	HIS82
C	ALA83
C	THR127

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEC C 502

Chain	Residue
C	TRP30
C	GLY33
C	HIS96
C	MET97
C	LYS99
C	SER105
C	LEU113
C	GLY117
C	VAL118
C	ILE120
C	HIS197
C	LEU201
C	SER206
C	SER207

---

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEC D 503

Chain	Residue
D	VAL100
D	CYS101
D	CYS104
D	HIS105
D	ASN169
D	ILE180
D	ARG184
D	TYR190
D	PHE218
D	ALA224
D	MET225
D	VAL228

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES E 504

Chain	Residue
E	CYS159
E	HIS161
E	LEU162
E	CYS178
E	HIS181
E	SER183

---

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SMA C 505

Chain	Residue
C	ILE125
C	ALA126
C	GLY143
C	VAL146
C	ILE147
C	LEU165
C	VAL270
C	PRO271
C	GLU272
C	PHE278
C	TYR279
C	MET295
P	HIS181

---

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEC N 521

Chain	Residue
N	GLN43
N	GLY47
N	ILE48
N	MET50
N	ARG79
N	HIS82
N	ALA83
N	PHE89
N	ALA128
N	GLY131
N	TYR132
N	VAL135
N	HIS183
N	TYR184
N	PRO187

---

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEC N 522

Chain	Residue
N	TRP30
N	GLY33
N	LEU36
N	HIS96
N	LYS99
N	SER105
N	LEU113
N	TRP114
N	GLY117
N	VAL194
N	HIS197
N	LEU201
N	SER206
N	SER207

---

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEC O 523

Chain	Residue
O	PHE218
O	ALA224
O	MET225
O	VAL100
O	CYS101
O	CYS104
O	HIS105
O	ASN169
O	PRO175
O	ARG184
O	TYR190
O	ILE191

---

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES P 524

Chain	Residue
P	CYS159
P	HIS161
P	LEU162
P	CYS178
P	CYS180
P	HIS181
P	SER183

---

site_id	BC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE SMA N 525

Chain	Residue
E	HIS181
N	THR122
N	ILE125
N	ALA126
N	PHE129
N	LEU130
N	MET139
N	VAL146
N	ILE147
N	ILE269
N	PRO271
N	GLU272
N	TYR279
N	MET295
N	PHE296

---

site_id	BC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEC W 526

Chain	Residue
W	ARG18
W	CYS19
W	CYS22
W	HIS23
W	VAL33
W	GLY34
W	ILE40
W	SER45
W	GLY46
W	TYR51
W	TYR53
W	THR54
W	ASN57
W	TRP64
W	TYR72
W	THR83
W	LYS84
W	MET85
W	PHE87

---

Functional Information from PROSITE/UniProt

site_id	PS00143
Number of Residues	23
Details	INSULINASE Insulinase family, zinc-binding region signature. Ggsryatkd.GvAHLLNRFnFqNT

Chain	Residue	Details
B	GLY37-THR59

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17761666","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	162
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8031140","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	366
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	208
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8031140","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	8
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KB9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P84","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IBZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PD4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00157","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	400
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9430684","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	234
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	306
Details	Domain: {"description":"Cytochrome c","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	74
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	18
Details	Compositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	4
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
Number of Residues	132
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI18
Number of Residues	294
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI19
Number of Residues	182
Details	Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI20
Number of Residues	6
Details	Region: {"description":"Hinge","evidences":[{"source":"PubMed","id":"30598556","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI21
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KB9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P84","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IBZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PD4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI22
Number of Residues	20
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI23
Number of Residues	2
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI24
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI25
Number of Residues	1
Details	Modified residue: {"description":"N6,N6,N6-trimethyllysine; by CTM1","evidences":[{"source":"PubMed","id":"10791961","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI26
Number of Residues	1
Details	Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"10821864","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ndo

Chain	Residue	Details
P	HIS181

---

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1ndo

Chain	Residue	Details
E	HIS181

---

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

Chain	Residue	Details
A	LYS73

---

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

Chain	Residue	Details
L	LYS73

---

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1ndo

Chain	Residue	Details
B	ASN52

---

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1ndo

Chain	Residue	Details
M	ASN52

---

site_id	MCSA1
Number of Residues	1
Details	M-CSA 208

Chain	Residue	Details
E	HIS181	covalently attached, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser
C	SER206	electrostatic stabiliser, hydrogen bond donor, radical stabiliser
C	LYS228	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser
C	ASP229	electrostatic stabiliser, hydrogen bond acceptor, radical stabiliser
C	GLU272	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser

---

site_id	MCSA2
Number of Residues	1
Details	M-CSA 208

Chain	Residue	Details
P	HIS181	covalently attached, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser
N	SER206	electrostatic stabiliser, hydrogen bond donor, radical stabiliser
N	LYS228	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser
N	ASP229	electrostatic stabiliser, hydrogen bond acceptor, radical stabiliser
N	GLU272	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser

---