Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4DL0

Crystal Structure of the heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0015078	molecular_function	proton transmembrane transporter activity
C	0033180	cellular_component	proton-transporting V-type ATPase, V1 domain
C	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
C	1902600	biological_process	proton transmembrane transport
E	0000139	cellular_component	Golgi membrane
E	0000221	cellular_component	vacuolar proton-transporting V-type ATPase, V1 domain
E	0000329	cellular_component	fungal-type vacuole membrane
E	0005515	molecular_function	protein binding
E	0005773	cellular_component	vacuole
E	0005774	cellular_component	vacuolar membrane
E	0006811	biological_process	monoatomic ion transport
E	0007035	biological_process	vacuolar acidification
E	0016020	cellular_component	membrane
E	0016471	cellular_component	vacuolar proton-transporting V-type ATPase complex
E	0033176	cellular_component	proton-transporting V-type ATPase complex
E	0033178	cellular_component	proton-transporting two-sector ATPase complex, catalytic domain
E	0045121	cellular_component	membrane raft
E	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
E	0048388	biological_process	endosomal lumen acidification
E	0061795	biological_process	Golgi lumen acidification
E	1902600	biological_process	proton transmembrane transport
G	0000139	cellular_component	Golgi membrane
G	0000221	cellular_component	vacuolar proton-transporting V-type ATPase, V1 domain
G	0000329	cellular_component	fungal-type vacuole membrane
G	0005515	molecular_function	protein binding
G	0005773	cellular_component	vacuole
G	0005774	cellular_component	vacuolar membrane
G	0006811	biological_process	monoatomic ion transport
G	0007035	biological_process	vacuolar acidification
G	0016020	cellular_component	membrane
G	0016471	cellular_component	vacuolar proton-transporting V-type ATPase complex
G	0016887	molecular_function	ATP hydrolysis activity
G	0033176	cellular_component	proton-transporting V-type ATPase complex
G	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
G	0048388	biological_process	endosomal lumen acidification
G	0061795	biological_process	Golgi lumen acidification
G	1902600	biological_process	proton transmembrane transport
I	0015078	molecular_function	proton transmembrane transporter activity
I	0033180	cellular_component	proton-transporting V-type ATPase, V1 domain
I	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
I	1902600	biological_process	proton transmembrane transport
J	0000139	cellular_component	Golgi membrane
J	0000221	cellular_component	vacuolar proton-transporting V-type ATPase, V1 domain
J	0000329	cellular_component	fungal-type vacuole membrane
J	0005515	molecular_function	protein binding
J	0005773	cellular_component	vacuole
J	0005774	cellular_component	vacuolar membrane
J	0006811	biological_process	monoatomic ion transport
J	0007035	biological_process	vacuolar acidification
J	0016020	cellular_component	membrane
J	0016471	cellular_component	vacuolar proton-transporting V-type ATPase complex
J	0033176	cellular_component	proton-transporting V-type ATPase complex
J	0033178	cellular_component	proton-transporting two-sector ATPase complex, catalytic domain
J	0045121	cellular_component	membrane raft
J	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
J	0048388	biological_process	endosomal lumen acidification
J	0061795	biological_process	Golgi lumen acidification
J	1902600	biological_process	proton transmembrane transport
K	0000139	cellular_component	Golgi membrane
K	0000221	cellular_component	vacuolar proton-transporting V-type ATPase, V1 domain
K	0000329	cellular_component	fungal-type vacuole membrane
K	0005515	molecular_function	protein binding
K	0005773	cellular_component	vacuole
K	0005774	cellular_component	vacuolar membrane
K	0006811	biological_process	monoatomic ion transport
K	0007035	biological_process	vacuolar acidification
K	0016020	cellular_component	membrane
K	0016471	cellular_component	vacuolar proton-transporting V-type ATPase complex
K	0016887	molecular_function	ATP hydrolysis activity
K	0033176	cellular_component	proton-transporting V-type ATPase complex
K	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
K	0048388	biological_process	endosomal lumen acidification
K	0061795	biological_process	Golgi lumen acidification
K	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 I 301

Chain	Residue
E	ILE45
E	ASN49
I	SER174
I	LEU175
I	ARG258
I	PHE260

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 K 201

Chain	Residue
K	ARG28
C	LYS166
J	LYS31
K	ARG25

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 K 202

Chain	Residue
C	ARG164
K	SER22
K	ARG25

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 K 203

Chain	Residue
C	ARG164
K	ARG25

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PBM J 301

Chain	Residue
C	GLU153
J	GLU221

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 301

Chain	Residue
C	SER174
C	LEU175
C	GLU259
J	ILE45

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 G 201

Chain	Residue
E	LYS31
E	ILE35
G	ARG25
G	ARG28
I	ARG164
I	LYS166

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 G 202

Chain	Residue
C	GLU189
G	ARG25
I	ARG164

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 G 203

Chain	Residue
G	HIS18
G	SER22
G	ARG25
I	ARG164

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PBM E 301

Chain	Residue
E	GLU221
I	GLU153

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Region: {"description":"Interaction with VMA5","evidences":[{"source":"PubMed","id":"15751969","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	38
Details	Region: {"description":"Interaction with VMA10","evidences":[{"source":"PubMed","id":"15751969","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	60
Details	Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Peters C."]}},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)