Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5ARE

Bovine mitochondrial ATP synthase state 1b

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0005886	cellular_component	plasma membrane
A	0006754	biological_process	ATP biosynthetic process
A	0006811	biological_process	monoatomic ion transport
A	0015986	biological_process	proton motive force-driven ATP synthesis
A	0016020	cellular_component	membrane
A	0032559	molecular_function	adenyl ribonucleotide binding
A	0043531	molecular_function	ADP binding
A	0045259	cellular_component	proton-transporting ATP synthase complex
A	0046034	biological_process	ATP metabolic process
A	0046872	molecular_function	metal ion binding
A	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
A	1902600	biological_process	proton transmembrane transport
B	0000166	molecular_function	nucleotide binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0005886	cellular_component	plasma membrane
B	0006754	biological_process	ATP biosynthetic process
B	0006811	biological_process	monoatomic ion transport
B	0015986	biological_process	proton motive force-driven ATP synthesis
B	0016020	cellular_component	membrane
B	0032559	molecular_function	adenyl ribonucleotide binding
B	0043531	molecular_function	ADP binding
B	0045259	cellular_component	proton-transporting ATP synthase complex
B	0046034	biological_process	ATP metabolic process
B	0046872	molecular_function	metal ion binding
B	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
B	1902600	biological_process	proton transmembrane transport
C	0000166	molecular_function	nucleotide binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0005886	cellular_component	plasma membrane
C	0006754	biological_process	ATP biosynthetic process
C	0006811	biological_process	monoatomic ion transport
C	0015986	biological_process	proton motive force-driven ATP synthesis
C	0016020	cellular_component	membrane
C	0032559	molecular_function	adenyl ribonucleotide binding
C	0043531	molecular_function	ADP binding
C	0045259	cellular_component	proton-transporting ATP synthase complex
C	0046034	biological_process	ATP metabolic process
C	0046872	molecular_function	metal ion binding
C	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
C	1902600	biological_process	proton transmembrane transport
D	0000166	molecular_function	nucleotide binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005743	cellular_component	mitochondrial inner membrane
D	0006754	biological_process	ATP biosynthetic process
D	0006811	biological_process	monoatomic ion transport
D	0015986	biological_process	proton motive force-driven ATP synthesis
D	0016020	cellular_component	membrane
D	0016887	molecular_function	ATP hydrolysis activity
D	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
D	0045259	cellular_component	proton-transporting ATP synthase complex
D	0046034	biological_process	ATP metabolic process
D	0046872	molecular_function	metal ion binding
D	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
D	1902600	biological_process	proton transmembrane transport
E	0000166	molecular_function	nucleotide binding
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0005743	cellular_component	mitochondrial inner membrane
E	0006754	biological_process	ATP biosynthetic process
E	0006811	biological_process	monoatomic ion transport
E	0015986	biological_process	proton motive force-driven ATP synthesis
E	0016020	cellular_component	membrane
E	0016887	molecular_function	ATP hydrolysis activity
E	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
E	0045259	cellular_component	proton-transporting ATP synthase complex
E	0046034	biological_process	ATP metabolic process
E	0046872	molecular_function	metal ion binding
E	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
E	1902600	biological_process	proton transmembrane transport
F	0000166	molecular_function	nucleotide binding
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005739	cellular_component	mitochondrion
F	0005743	cellular_component	mitochondrial inner membrane
F	0006754	biological_process	ATP biosynthetic process
F	0006811	biological_process	monoatomic ion transport
F	0015986	biological_process	proton motive force-driven ATP synthesis
F	0016020	cellular_component	membrane
F	0016887	molecular_function	ATP hydrolysis activity
F	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
F	0045259	cellular_component	proton-transporting ATP synthase complex
F	0046034	biological_process	ATP metabolic process
F	0046872	molecular_function	metal ion binding
F	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
F	1902600	biological_process	proton transmembrane transport
G	0005515	molecular_function	protein binding
G	0005739	cellular_component	mitochondrion
G	0005743	cellular_component	mitochondrial inner membrane
G	0006754	biological_process	ATP biosynthetic process
G	0006811	biological_process	monoatomic ion transport
G	0015986	biological_process	proton motive force-driven ATP synthesis
G	0016020	cellular_component	membrane
G	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
G	0045259	cellular_component	proton-transporting ATP synthase complex
G	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
G	1902600	biological_process	proton transmembrane transport
H	0015986	biological_process	proton motive force-driven ATP synthesis
H	0045259	cellular_component	proton-transporting ATP synthase complex
H	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
I	0005739	cellular_component	mitochondrion
I	0005743	cellular_component	mitochondrial inner membrane
I	0006754	biological_process	ATP biosynthetic process
I	0006811	biological_process	monoatomic ion transport
I	0015986	biological_process	proton motive force-driven ATP synthesis
I	0016020	cellular_component	membrane
I	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
I	0045259	cellular_component	proton-transporting ATP synthase complex
I	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
I	1902600	biological_process	proton transmembrane transport
J	0015078	molecular_function	proton transmembrane transporter activity
J	0015986	biological_process	proton motive force-driven ATP synthesis
J	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
J	0045259	cellular_component	proton-transporting ATP synthase complex
J	1902600	biological_process	proton transmembrane transport
K	0015078	molecular_function	proton transmembrane transporter activity
K	0015986	biological_process	proton motive force-driven ATP synthesis
K	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
K	0045259	cellular_component	proton-transporting ATP synthase complex
K	1902600	biological_process	proton transmembrane transport
L	0015078	molecular_function	proton transmembrane transporter activity
L	0015986	biological_process	proton motive force-driven ATP synthesis
L	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
L	0045259	cellular_component	proton-transporting ATP synthase complex
L	1902600	biological_process	proton transmembrane transport
M	0015078	molecular_function	proton transmembrane transporter activity
M	0015986	biological_process	proton motive force-driven ATP synthesis
M	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
M	0045259	cellular_component	proton-transporting ATP synthase complex
M	1902600	biological_process	proton transmembrane transport
N	0015078	molecular_function	proton transmembrane transporter activity
N	0015986	biological_process	proton motive force-driven ATP synthesis
N	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
N	0045259	cellular_component	proton-transporting ATP synthase complex
N	1902600	biological_process	proton transmembrane transport
O	0015078	molecular_function	proton transmembrane transporter activity
O	0015986	biological_process	proton motive force-driven ATP synthesis
O	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
O	0045259	cellular_component	proton-transporting ATP synthase complex
O	1902600	biological_process	proton transmembrane transport
P	0015078	molecular_function	proton transmembrane transporter activity
P	0015986	biological_process	proton motive force-driven ATP synthesis
P	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
P	0045259	cellular_component	proton-transporting ATP synthase complex
P	1902600	biological_process	proton transmembrane transport
Q	0015078	molecular_function	proton transmembrane transporter activity
Q	0015986	biological_process	proton motive force-driven ATP synthesis
Q	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
Q	0045259	cellular_component	proton-transporting ATP synthase complex
Q	1902600	biological_process	proton transmembrane transport
S	0015986	biological_process	proton motive force-driven ATP synthesis
S	0016020	cellular_component	membrane
S	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
T	0015078	molecular_function	proton transmembrane transporter activity
T	0015986	biological_process	proton motive force-driven ATP synthesis
U	0015078	molecular_function	proton transmembrane transporter activity
U	0015986	biological_process	proton motive force-driven ATP synthesis
U	0045259	cellular_component	proton-transporting ATP synthase complex
V	0015078	molecular_function	proton transmembrane transporter activity
V	0015986	biological_process	proton motive force-driven ATP synthesis
V	0045259	cellular_component	proton-transporting ATP synthase complex
W	0005739	cellular_component	mitochondrion
W	0005743	cellular_component	mitochondrial inner membrane
W	0006754	biological_process	ATP biosynthetic process
W	0006811	biological_process	monoatomic ion transport
W	0015078	molecular_function	proton transmembrane transporter activity
W	0015252	molecular_function	proton channel activity
W	0015986	biological_process	proton motive force-driven ATP synthesis
W	0016020	cellular_component	membrane
W	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
W	0045259	cellular_component	proton-transporting ATP synthase complex
W	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
W	1902600	biological_process	proton transmembrane transport

Functional Information from PROSITE/UniProt

site_id	PS00152
Number of Residues	10
Details	ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS

Chain	Residue	Details
A	PRO363-SER372
D	PRO346-SER355

site_id	PS00153
Number of Residues	14
Details	ATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA

Chain	Residue	Details
G	ILE258-ALA271

site_id	PS00389
Number of Residues	20
Details	ATPASE_DELTA ATP synthase delta (OSCP) subunit signature. LkLevkIDpSImGGMIVRiG

Chain	Residue	Details
S	LEU148-GLY167

site_id	PS00449
Number of Residues	10
Details	ATPASE_A ATP synthase a subunit signature. ALAVRLTANI

Chain	Residue	Details
W	ALA155-ILE164

site_id	PS00605
Number of Residues	22
Details	ATPASE_C ATP synthase c subunit signature. ARNPslkqqLfSyaILgfaLsE

Chain	Residue	Details
J	ALA37-GLU58

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17895376","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8065448","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8790345","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9687365","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BMF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1COW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E1Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E1R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E79","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EFR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1H8H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NBM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OHH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CK3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JDI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JIZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JJ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JJ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V7Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WSS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XND","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TSF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TT3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YXW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Z1M","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Site: {"description":"Required for activity","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine; alternate","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	15
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P15999","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	33
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	3
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	3
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine; alternate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17895376","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9687365","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V7Q","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9687365","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PDB","id":"1E1R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1H8E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ASU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TSF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	15
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P56480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06576","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P56480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06576","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10719","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	3
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P36542","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P36542","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D3D9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	3
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P56382","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56382","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	420
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	8
Details	Site: {"description":"Reversibly protonated during proton transport","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	8
Details	Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"UniProtKB","id":"P05496","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	5
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DB20","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9DB20","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	3
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9DB20","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P48047","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQQ7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQQ7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P24539","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DCX2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	3
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9DCX2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O75947","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI43
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P18859","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI44
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P97450","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI45
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P97450","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 178

Chain	Residue	Details
D	LYS162	electrostatic stabiliser
D	GLU188	electrostatic stabiliser
D	ARG189	electrostatic stabiliser

site_id	MCSA2
Number of Residues	3
Details	M-CSA 178

Chain	Residue	Details
E	LYS162	electrostatic stabiliser
E	GLU188	electrostatic stabiliser
E	ARG189	electrostatic stabiliser

site_id	MCSA3
Number of Residues	3
Details	M-CSA 178

Chain	Residue	Details
F	LYS162	electrostatic stabiliser
F	GLU188	electrostatic stabiliser
F	ARG189	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)