3IBG

Crystal structure of Aspergillus fumigatus Get3 with bound ADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0042802	molecular_function	identical protein binding
A	0043529	cellular_component	GET complex
A	0045048	biological_process	protein insertion into ER membrane
A	0046872	molecular_function	metal ion binding
A	0071816	biological_process	tail-anchored membrane protein insertion into ER membrane
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0042802	molecular_function	identical protein binding
B	0043529	cellular_component	GET complex
B	0045048	biological_process	protein insertion into ER membrane
B	0046872	molecular_function	metal ion binding
B	0071816	biological_process	tail-anchored membrane protein insertion into ER membrane
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005783	cellular_component	endoplasmic reticulum
C	0016787	molecular_function	hydrolase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0042802	molecular_function	identical protein binding
C	0043529	cellular_component	GET complex
C	0045048	biological_process	protein insertion into ER membrane
C	0046872	molecular_function	metal ion binding
C	0071816	biological_process	tail-anchored membrane protein insertion into ER membrane
D	0000166	molecular_function	nucleotide binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005783	cellular_component	endoplasmic reticulum
D	0016787	molecular_function	hydrolase activity
D	0016887	molecular_function	ATP hydrolysis activity
D	0042802	molecular_function	identical protein binding
D	0043529	cellular_component	GET complex
D	0045048	biological_process	protein insertion into ER membrane
D	0046872	molecular_function	metal ion binding
D	0071816	biological_process	tail-anchored membrane protein insertion into ER membrane
E	0000166	molecular_function	nucleotide binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005783	cellular_component	endoplasmic reticulum
E	0016787	molecular_function	hydrolase activity
E	0016887	molecular_function	ATP hydrolysis activity
E	0042802	molecular_function	identical protein binding
E	0043529	cellular_component	GET complex
E	0045048	biological_process	protein insertion into ER membrane
E	0046872	molecular_function	metal ion binding
E	0071816	biological_process	tail-anchored membrane protein insertion into ER membrane
F	0000166	molecular_function	nucleotide binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005783	cellular_component	endoplasmic reticulum
F	0016787	molecular_function	hydrolase activity
F	0016887	molecular_function	ATP hydrolysis activity
F	0042802	molecular_function	identical protein binding
F	0043529	cellular_component	GET complex
F	0045048	biological_process	protein insertion into ER membrane
F	0046872	molecular_function	metal ion binding
F	0071816	biological_process	tail-anchored membrane protein insertion into ER membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ADP A 349

Chain	Residue
A	GLY36
A	VAL319
A	ARG320
A	PHE328
F	ARG200
A	GLY38
A	LYS39
A	THR40
A	THR41
A	ASN67
A	ASN272
A	PRO313
A	LEU315

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADP B 349

Chain	Residue
B	GLY36
B	VAL37
B	GLY38
B	LYS39
B	THR40
B	THR41
B	ASN67
B	ASN272
B	PRO313
B	LEU314
B	LEU315
B	VAL319
B	ARG320
B	PHE328
C	ARG200

---

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP C 349

Chain	Residue
B	ARG200
C	GLY36
C	VAL37
C	GLY38
C	LYS39
C	THR40
C	THR41
C	ASN67
C	ASN272
C	PRO313
C	LEU314
C	LEU315
C	GLU318
C	VAL319
C	ARG320
C	PHE328

---

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP D 349

Chain	Residue
D	GLY36
D	VAL37
D	GLY38
D	LYS39
D	THR40
D	THR41
D	ASN67
D	ASN272
D	PRO313
D	LEU314
D	LEU315
D	GLU318
D	VAL319
D	ARG320
D	PHE328
E	ARG200

---

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ADP E 349

Chain	Residue
D	ARG200
E	GLY36
E	GLY38
E	LYS39
E	THR40
E	THR41
E	ASN67
E	ASN272
E	PRO313
E	LEU314
E	LEU315
E	VAL319
E	ARG320
E	PHE328

---

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADP F 349

Chain	Residue
A	ARG200
F	GLY36
F	VAL37
F	GLY38
F	LYS39
F	THR40
F	THR41
F	ASN67
F	ASN272
F	PRO313
F	LEU315
F	GLU318
F	VAL319
F	ARG320
F	PHE328

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03112","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	54
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03112","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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