Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4UJ3

Crystal structure of human Rab11-Rabin8-FIP3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003924	molecular_function	GTPase activity
A	0005525	molecular_function	GTP binding
B	0005085	molecular_function	guanyl-nucleotide exchange factor activity
D	0003924	molecular_function	GTPase activity
D	0005525	molecular_function	GTP binding
E	0005085	molecular_function	guanyl-nucleotide exchange factor activity
G	0003924	molecular_function	GTPase activity
G	0005525	molecular_function	GTP binding
H	0005085	molecular_function	guanyl-nucleotide exchange factor activity
J	0003924	molecular_function	GTPase activity
J	0005525	molecular_function	GTP binding
K	0005085	molecular_function	guanyl-nucleotide exchange factor activity
M	0003924	molecular_function	GTPase activity
M	0005525	molecular_function	GTP binding
N	0005085	molecular_function	guanyl-nucleotide exchange factor activity
P	0003924	molecular_function	GTPase activity
P	0005525	molecular_function	GTP binding
Q	0005085	molecular_function	guanyl-nucleotide exchange factor activity
S	0003924	molecular_function	GTPase activity
S	0005525	molecular_function	GTP binding
T	0005085	molecular_function	guanyl-nucleotide exchange factor activity
V	0003924	molecular_function	GTPase activity
V	0005525	molecular_function	GTP binding
W	0005085	molecular_function	guanyl-nucleotide exchange factor activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE GNP A 200

Chain	Residue
A	SER20
A	LEU38
A	SER40
A	SER42
A	THR43
A	GLY69
A	ASN124
A	LYS125
A	ASP127
A	LEU128
A	SER154
A	GLY21
A	ALA155
A	LEU156
A	MG201
B	TYR423
A	VAL22
A	GLY23
A	LYS24
A	SER25
A	ASN26
A	PHE36
A	ASN37

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 201

Chain	Residue
A	SER25
A	THR43
A	GNP200

site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE GNP D 200

Chain	Residue
D	SER20
D	GLY21
D	VAL22
D	GLY23
D	LYS24
D	SER25
D	ASN26
D	PHE36
D	ASN37
D	LEU38
D	SER40
D	SER42
D	THR43
D	THR67
D	GLY69
D	ASN124
D	LYS125
D	ASP127
D	LEU128
D	SER154
D	ALA155
D	LEU156
D	MG201
E	TYR423

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 201

Chain	Residue
D	SER25
D	THR43
D	ASP66
D	GNP200

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GNP G 200

Chain	Residue
G	SER20
G	GLY21
G	GLY23
G	LYS24
G	SER25
G	ASN26
G	ASN37
G	LEU38
G	SER40
G	SER42
G	THR43
G	GLY69
G	ASN124
G	LYS125
G	ASP127
G	LEU128
G	SER154
G	ALA155
G	LEU156
G	MG201
H	TYR423

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG G 201

Chain	Residue
G	SER25
G	THR43
G	ASP66
G	THR67
G	GNP200

site_id	AC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE GNP J 200

Chain	Residue
J	ALA155
J	LEU156
J	MG201
K	TYR423
J	SER20
J	GLY21
J	VAL22
J	GLY23
J	LYS24
J	SER25
J	ASN26
J	PHE36
J	ASN37
J	LEU38
J	SER40
J	SER42
J	THR43
J	GLY69
J	ASN124
J	LYS125
J	ASP127
J	LEU128
J	SER154

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG J 201

Chain	Residue
J	SER25
J	THR43
J	ASP66
J	THR67
J	GNP200

site_id	AC9
Number of Residues	25
Details	BINDING SITE FOR RESIDUE GNP M 200

Chain	Residue
M	SER20
M	GLY21
M	VAL22
M	GLY23
M	LYS24
M	SER25
M	ASN26
M	PHE36
M	ASN37
M	LEU38
M	SER40
M	SER42
M	THR43
M	THR67
M	ALA68
M	GLY69
M	ASN124
M	LYS125
M	ASP127
M	LEU128
M	SER154
M	ALA155
M	LEU156
M	MG201
N	TYR423

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG M 201

Chain	Residue
M	SER25
M	THR43
M	ASP66
M	THR67
M	GNP200

site_id	BC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE GNP P 200

Chain	Residue
P	ASP19
P	SER20
P	GLY21
P	VAL22
P	GLY23
P	LYS24
P	SER25
P	ASN26
P	PHE36
P	ASN37
P	LEU38
P	SER42
P	THR43
P	THR67
P	GLY69
P	ASN124
P	LYS125
P	ASP127
P	LEU128
P	SER154
P	ALA155
P	LEU156
P	MG201

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG P 201

Chain	Residue
P	SER25
P	THR43
P	ASP66
P	THR67
P	GNP200

site_id	BC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE GNP S 200

Chain	Residue
S	SER20
S	GLY21
S	VAL22
S	GLY23
S	LYS24
S	SER25
S	ASN26
S	PHE36
S	ASN37
S	LEU38
S	SER40
S	SER42
S	THR43
S	THR67
S	GLY69
S	ASN124
S	LYS125
S	ASP127
S	LEU128
S	SER154
S	ALA155
S	LEU156
S	MG201
T	TYR423

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG S 201

Chain	Residue
S	LYS24
S	SER25
S	THR43
S	ASP66
S	THR67
S	GNP200

site_id	BC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE GNP V 200

Chain	Residue
V	ASP19
V	SER20
V	GLY21
V	VAL22
V	GLY23
V	LYS24
V	SER25
V	ASN26
V	ASN37
V	LEU38
V	SER40
V	SER42
V	THR43
V	THR67
V	GLY69
V	ASN124
V	LYS125
V	ASP127
V	LEU128
V	SER154
V	ALA155
V	LEU156
V	MG201
V	PG4300
W	TYR423

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG V 201

Chain	Residue
V	SER25
V	THR43
V	GNP200

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PG4 V 300

Chain	Residue
V	GNP200
W	THR419
W	TYR420
W	TYR423
W	GLU440

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 M 1182

Chain	Residue
M	ARG140
M	PHE150
M	ILE151
Q	GLU372
Q	ASN399
Q	TYR401

Functional Information from PROSITE/UniProt

site_id	PS00014
Number of Residues	4
Details	ER_TARGET Endoplasmic reticulum targeting sequence. KEEL

Chain	Residue	Details
B	LYS457-LEU460

site_id	PS00675
Number of Residues	14
Details	SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VVLiGDSGVGKsnL

Chain	Residue	Details
A	VAL14-LEU27

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
B	SER272
J	GLY18
J	ASN124
J	SER154
M	GLY18
M	ASN124
M	SER154
P	GLY18
P	ASN124
P	SER154
S	GLY18
E	SER272
S	ASN124
S	SER154
V	GLY18
V	ASN124
V	SER154
H	SER272
K	SER272
N	SER272
Q	SER272
T	SER272
W	SER272
G	SER154

site_id	SWS_FT_FI2
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q68EF0

Chain	Residue	Details
B	SER280
E	SER280
H	SER280
K	SER280
N	SER280
Q	SER280
T	SER280
W	SER280

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:16905101, ECO:0000269\|PubMed:17007872, ECO:0000269\|PubMed:17030804, ECO:0007744\|PDB:1OIW, ECO:0007744\|PDB:4D0L, ECO:0007744\|PDB:4D0M, ECO:0007744\|PDB:5C46, ECO:0007744\|PDB:5FBL

Chain	Residue	Details
A	ASP66
D	ASP66
G	ASP66
J	ASP66
M	ASP66
P	ASP66
S	ASP66
V	ASP66

site_id	SWS_FT_FI4
Number of Residues	8
Details	CARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269\|PubMed:32974215

Chain	Residue	Details
A	ARG4
D	ARG4
G	ARG4
J	ARG4
M	ARG4
P	ARG4
S	ARG4
V	ARG4

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