4EFA

Crystal Structure of the Heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase - second conformation

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	0005774	cellular_component	vacuolar membrane
E	0006811	biological_process	monoatomic ion transport
E	0007035	biological_process	vacuolar acidification
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	0005774	cellular_component	vacuolar membrane
G	0006811	biological_process	monoatomic ion transport
G	0007035	biological_process	vacuolar acidification
G	0016471	cellular_component	vacuolar proton-transporting V-type ATPase complex
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 301

Chain	Residue
C	LEU175
C	ARG258
C	GLU259

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 G 201

Chain	Residue
G	ARG25

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

Chain	Residue
E	LYS31
G	ARG25
G	ARG28

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 G 203

Chain	Residue
G	ARG25
G	HIS18
G	SER22

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	12
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	19
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	30
Details	Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
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

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