Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1TU3

Crystal Structure of Rab5 complex with Rabaptin5 C-terminal Domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003924	molecular_function	GTPase activity
A	0005525	molecular_function	GTP binding
B	0003924	molecular_function	GTPase activity
B	0005525	molecular_function	GTP binding
C	0003924	molecular_function	GTPase activity
C	0005525	molecular_function	GTP binding
D	0003924	molecular_function	GTPase activity
D	0005525	molecular_function	GTP binding
E	0003924	molecular_function	GTPase activity
E	0005525	molecular_function	GTP binding
F	0005096	molecular_function	GTPase activator activity
F	0006897	biological_process	endocytosis
G	0005096	molecular_function	GTPase activator activity
G	0006897	biological_process	endocytosis
H	0005096	molecular_function	GTPase activator activity
H	0006897	biological_process	endocytosis
I	0005096	molecular_function	GTPase activator activity
I	0006897	biological_process	endocytosis
J	0005096	molecular_function	GTPase activator activity
J	0006897	biological_process	endocytosis

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1201

Chain	Residue
A	SER34
A	THR52
A	HOH404
A	HOH405
A	GNP1202

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 2201

Chain	Residue
B	GNP2202
B	SER34
B	THR52
B	HOH420
B	HOH421

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 3201

Chain	Residue
C	SER34
C	THR52
C	HOH431
C	HOH432
C	GNP3202

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 4201

Chain	Residue
D	SER34
D	THR52
D	HOH440
D	HOH441
D	GNP4202

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 5201

Chain	Residue
E	SER34
E	THR52
E	HOH450
E	HOH451
E	GNP5202

site_id	AC6
Number of Residues	27
Details	BINDING SITE FOR RESIDUE GNP A 1202

Chain	Residue
A	SER29
A	ALA30
A	VAL31
A	GLY32
A	LYS33
A	SER34
A	SER35
A	PHE45
A	HIS46
A	GLU47
A	GLN49
A	GLU50
A	SER51
A	THR52
A	GLY78
A	ASN133
A	LYS134
A	ASP136
A	LEU137
A	SER163
A	ALA164
A	LYS165
A	HOH403
A	HOH404
A	HOH405
A	HOH592
A	MG1201

site_id	AC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE GNP B 2202

Chain	Residue
B	SER29
B	ALA30
B	VAL31
B	GLY32
B	LYS33
B	SER34
B	SER35
B	PHE45
B	HIS46
B	GLU47
B	GLN49
B	SER51
B	THR52
B	GLY78
B	ASN133
B	LYS134
B	ASP136
B	LEU137
B	SER163
B	ALA164
B	LYS165
B	HOH420
B	HOH421
B	MG2201

site_id	AC8
Number of Residues	23
Details	BINDING SITE FOR RESIDUE GNP C 3202

Chain	Residue
C	SER29
C	ALA30
C	VAL31
C	GLY32
C	LYS33
C	SER34
C	SER35
C	PHE45
C	HIS46
C	GLU47
C	GLN49
C	SER51
C	THR52
C	GLY78
C	ASN133
C	LYS134
C	ASP136
C	SER163
C	ALA164
C	LYS165
C	HOH431
C	HOH432
C	MG3201

site_id	AC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE GNP D 4202

Chain	Residue
D	SER29
D	ALA30
D	VAL31
D	GLY32
D	LYS33
D	SER34
D	SER35
D	PHE45
D	GLN49
D	GLU50
D	SER51
D	THR52
D	GLY78
D	ASN133
D	LYS134
D	ASP136
D	LEU137
D	SER163
D	ALA164
D	LYS165
D	HOH440
D	HOH441
D	HOH442
D	MG4201

site_id	BC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE GNP E 5202

Chain	Residue
E	SER29
E	ALA30
E	VAL31
E	GLY32
E	LYS33
E	SER34
E	SER35
E	PHE45
E	HIS46
E	GLU47
E	GLN49
E	SER51
E	THR52
E	GLY78
E	ASN133
E	LYS134
E	ASP136
E	LEU137
E	SER163
E	ALA164
E	LYS165
E	HOH450
E	HOH451
E	HOH454
E	MG5201

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	25
Details	BINDING: BINDING => ECO:0000269\|PubMed:12433916, ECO:0000269\|PubMed:14684892, ECO:0000269\|PubMed:15378032, ECO:0000269\|PubMed:20534488, ECO:0007744\|PDB:1N6H, ECO:0007744\|PDB:1N6L, ECO:0007744\|PDB:1N6N, ECO:0007744\|PDB:1N6O, ECO:0007744\|PDB:1N6P, ECO:0007744\|PDB:1N6R, ECO:0007744\|PDB:1R2Q, ECO:0007744\|PDB:1TU3, ECO:0007744\|PDB:3MJH

Chain	Residue	Details
A	GLY27
B	SER163
C	GLY27
C	HIS46
C	ASP75
C	ASN133
C	SER163
D	GLY27
D	HIS46
D	ASP75
D	ASN133
A	HIS46
D	SER163
E	GLY27
E	HIS46
E	ASP75
E	ASN133
E	SER163
A	ASP75
A	ASN133
A	SER163
B	GLY27
B	HIS46
B	ASP75
B	ASN133

site_id	SWS_FT_FI2
Number of Residues	5
Details	MOD_RES: Phosphoserine; by LRRK2 => ECO:0000269\|PubMed:29125462

Chain	Residue	Details
A	SER84
B	SER84
C	SER84
D	SER84
E	SER84

site_id	SWS_FT_FI3
Number of Residues	5
Details	CARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269\|PubMed:32974215

Chain	Residue	Details
A	ARG120
B	ARG120
C	ARG120
D	ARG120
E	ARG120

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLN79

site_id	CSA10
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
E	ALA30

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

Chain	Residue	Details
B	GLN79

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

Chain	Residue	Details
C	GLN79

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

Chain	Residue	Details
D	GLN79

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

Chain	Residue	Details
E	GLN79

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

Chain	Residue	Details
A	ALA30

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

Chain	Residue	Details
B	ALA30

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

Chain	Residue	Details
C	ALA30

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

Chain	Residue	Details
D	ALA30

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