Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3MPW

Structure of EUTM in 2-D protein membrane

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005198	molecular_function	structural molecule activity
A	0031469	cellular_component	bacterial microcompartment
A	0031471	cellular_component	ethanolamine degradation polyhedral organelle
A	0034214	biological_process	protein hexamerization
A	0042802	molecular_function	identical protein binding
A	0046336	biological_process	ethanolamine catabolic process
B	0005198	molecular_function	structural molecule activity
B	0031469	cellular_component	bacterial microcompartment
B	0031471	cellular_component	ethanolamine degradation polyhedral organelle
B	0034214	biological_process	protein hexamerization
B	0042802	molecular_function	identical protein binding
B	0046336	biological_process	ethanolamine catabolic process
C	0005198	molecular_function	structural molecule activity
C	0031469	cellular_component	bacterial microcompartment
C	0031471	cellular_component	ethanolamine degradation polyhedral organelle
C	0034214	biological_process	protein hexamerization
C	0042802	molecular_function	identical protein binding
C	0046336	biological_process	ethanolamine catabolic process
D	0005198	molecular_function	structural molecule activity
D	0031469	cellular_component	bacterial microcompartment
D	0031471	cellular_component	ethanolamine degradation polyhedral organelle
D	0034214	biological_process	protein hexamerization
D	0042802	molecular_function	identical protein binding
D	0046336	biological_process	ethanolamine catabolic process
E	0005198	molecular_function	structural molecule activity
E	0031469	cellular_component	bacterial microcompartment
E	0031471	cellular_component	ethanolamine degradation polyhedral organelle
E	0034214	biological_process	protein hexamerization
E	0042802	molecular_function	identical protein binding
E	0046336	biological_process	ethanolamine catabolic process
F	0005198	molecular_function	structural molecule activity
F	0031469	cellular_component	bacterial microcompartment
F	0031471	cellular_component	ethanolamine degradation polyhedral organelle
F	0034214	biological_process	protein hexamerization
F	0042802	molecular_function	identical protein binding
F	0046336	biological_process	ethanolamine catabolic process
G	0005198	molecular_function	structural molecule activity
G	0031469	cellular_component	bacterial microcompartment
G	0031471	cellular_component	ethanolamine degradation polyhedral organelle
G	0034214	biological_process	protein hexamerization
G	0042802	molecular_function	identical protein binding
G	0046336	biological_process	ethanolamine catabolic process
H	0005198	molecular_function	structural molecule activity
H	0031469	cellular_component	bacterial microcompartment
H	0031471	cellular_component	ethanolamine degradation polyhedral organelle
H	0034214	biological_process	protein hexamerization
H	0042802	molecular_function	identical protein binding
H	0046336	biological_process	ethanolamine catabolic process
I	0005198	molecular_function	structural molecule activity
I	0031469	cellular_component	bacterial microcompartment
I	0031471	cellular_component	ethanolamine degradation polyhedral organelle
I	0034214	biological_process	protein hexamerization
I	0042802	molecular_function	identical protein binding
I	0046336	biological_process	ethanolamine catabolic process
J	0005198	molecular_function	structural molecule activity
J	0031469	cellular_component	bacterial microcompartment
J	0031471	cellular_component	ethanolamine degradation polyhedral organelle
J	0034214	biological_process	protein hexamerization
J	0042802	molecular_function	identical protein binding
J	0046336	biological_process	ethanolamine catabolic process
K	0005198	molecular_function	structural molecule activity
K	0031469	cellular_component	bacterial microcompartment
K	0031471	cellular_component	ethanolamine degradation polyhedral organelle
K	0034214	biological_process	protein hexamerization
K	0042802	molecular_function	identical protein binding
K	0046336	biological_process	ethanolamine catabolic process
L	0005198	molecular_function	structural molecule activity
L	0031469	cellular_component	bacterial microcompartment
L	0031471	cellular_component	ethanolamine degradation polyhedral organelle
L	0034214	biological_process	protein hexamerization
L	0042802	molecular_function	identical protein binding
L	0046336	biological_process	ethanolamine catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 155

Chain	Residue
A	GLY38
B	GLY38
C	GLY38
E	GLY38
F	GLY38

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PO4 I 156

Chain	Residue
I	GLY38

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 D 200

Chain	Residue
D	GLU2
D	ARG77

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 E 201

Chain	Residue
E	ALA3
E	PRO76
E	ARG77
E	PRO78
E	GLU2

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PO4 F 202

Chain	Residue
F	GLU2

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 203

Chain	Residue
A	GLU2
A	PRO76
A	ARG77

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 B 204

Chain	Residue
B	GLU2
B	ALA3

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PO4 C 205

Chain	Residue
C	GLU2

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 G 206

Chain	Residue
G	GLU2
G	PRO76
G	ARG77

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 H 207

Chain	Residue
H	GLU2
H	ALA3
H	ARG46

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 I 208

Chain	Residue
I	GLU2
I	PRO76
I	ARG77
I	PRO78
K	LYS24

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 J 209

Chain	Residue
J	GLU2
J	PRO76
J	ARG77

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 K 210

Chain	Residue
K	GLU2
K	PRO76
K	ARG77
K	PRO78

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 L 211

Chain	Residue
H	LYS24
L	GLU2
L	ARG77

Functional Information from PROSITE/UniProt

site_id	PS01139
Number of Residues	20
Details	BMC_1 Bacterial microcompartment (BMC) domain signature. DaMvKAArVkLVGvkqiGGG

Chain	Residue	Details
G	ASP20-GLY39

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1008
Details	Domain: {"description":"BMC","evidences":[{"source":"PROSITE-ProRule","id":"PRU01278","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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