Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1E1Q

BOVINE MITOCHONDRIAL F1-ATPASE AT 100K

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	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	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	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	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	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	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	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 601

Chain	Residue
A	THR176
A	ANP600
A	HOH2043

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 601

Chain	Residue
B	THR176
B	ANP600

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 601

Chain	Residue
C	THR176
C	ANP600
C	HOH2035

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 601

Chain	Residue
D	ADP600
D	HOH2037
D	THR163

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 E 602

Chain	Residue
E	ALA158
E	GLY159
E	VAL160
E	GLY161
E	LYS162
E	THR163

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 601

Chain	Residue
F	THR163
F	ANP600
F	HOH2107

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ANP A 600

Chain	Residue
A	ARG171
A	GLN172
A	THR173
A	GLY174
A	LYS175
A	THR176
A	SER177
A	PHE357
A	ARG362
A	PRO363
A	GLN430
A	GLN432
A	MG601
A	HOH2029
A	HOH2099
A	HOH2100

site_id	AC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ANP B 600

Chain	Residue
B	ARG171
B	GLN172
B	THR173
B	GLY174
B	LYS175
B	THR176
B	SER177
B	PHE357
B	ARG362
B	PRO363
B	GLN430
B	GLN432
B	MG601
B	HOH2024
B	HOH2082
B	HOH2083
E	ASP359

site_id	AC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ANP C 600

Chain	Residue
C	ARG171
C	GLN172
C	THR173
C	GLY174
C	LYS175
C	THR176
C	SER177
C	PHE357
C	ARG362
C	GLN430
C	GLN432
C	MG601
C	HOH2035
C	HOH2074
C	HOH2106
C	HOH2108
C	HOH2109
F	HOH2097

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP D 600

Chain	Residue
C	SER372
C	ARG373
D	GLY159
D	VAL160
D	GLY161
D	LYS162
D	THR163
D	VAL164
D	TYR345
D	PHE418
D	ALA421
D	PHE424
D	MG601
D	HOH2087
D	HOH2091
D	HOH2092

site_id	BC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ANP F 600

Chain	Residue
F	PHE418
F	ALA421
F	PHE424
F	THR425
F	MG601
F	HOH2040
F	HOH2101
F	HOH2106
F	HOH2107
B	ILE343
B	SER344
B	VAL371
B	ARG373
F	ALA158
F	GLY159
F	GLY161
F	LYS162
F	THR163
F	VAL164
F	ARG189
F	TYR345

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

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	3
Details	Modified residue: {"description":"Phosphoserine; alternate","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","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
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_FI6
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P15999","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
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_FI8
Number of Residues	7
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P25705","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	1
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	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
D	ARG356

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

Chain	Residue	Details
E	ARG356

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

Chain	Residue	Details
F	ARG356

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
C	ARG373
D	ARG189
D	GLU188
D	LYS162

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
A	ARG373
E	ARG189
E	GLU188
E	LYS162

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
F	ARG189
F	GLU188
F	LYS162
B	ARG373

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

Chain	Residue	Details
A	LYS175
A	LYS209
A	GLN208

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

Chain	Residue	Details
B	LYS175
B	LYS209
B	GLN208

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
C	LYS175
C	LYS209
C	GLN208

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)