Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4LHW

Crystal structure of Rab8 in its active GppNHp-bound form

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 301

Chain	Residue
A	THR22
A	THR40
A	GNP302
A	HOH402
A	HOH425

site_id	AC2
Number of Residues	33
Details	BINDING SITE FOR RESIDUE GNP A 302

Chain	Residue
A	LYS21
A	THR22
A	CYS23
A	PHE33
A	ASN34
A	SER35
A	THR36
A	PHE37
A	SER39
A	THR40
A	ALA65
A	GLY66
A	ASN121
A	LYS122
A	ASP124
A	VAL125
A	SER151
A	ALA152
A	LYS153
A	MG301
A	HOH402
A	HOH414
A	HOH425
A	HOH475
A	HOH486
A	HOH551
A	HOH557
A	HOH590
A	HOH626
A	SER17
A	GLY18
A	VAL19
A	GLY20

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD A 303

Chain	Residue
A	TRP62
A	TYR77
A	GLY80
B	ILE73
B	TYR77
B	HOH302

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 201

Chain	Residue
B	THR22
B	THR40
B	GNP202
B	HOH322
B	HOH327

site_id	AC5
Number of Residues	29
Details	BINDING SITE FOR RESIDUE GNP B 202

Chain	Residue
B	SER17
B	GLY18
B	VAL19
B	GLY20
B	LYS21
B	THR22
B	CYS23
B	PHE33
B	ASN34
B	SER35
B	THR36
B	PHE37
B	SER39
B	THR40
B	GLY66
B	ASN121
B	LYS122
B	ASP124
B	VAL125
B	SER151
B	ALA152
B	LYS153
B	MG201
B	HOH307
B	HOH322
B	HOH326
B	HOH327
B	HOH455
D	HOH428

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

Chain	Residue
C	THR22
C	THR40
C	GNP202
C	HOH307
C	HOH318

site_id	AC7
Number of Residues	30
Details	BINDING SITE FOR RESIDUE GNP C 202

Chain	Residue
C	ALA152
C	LYS153
C	MG201
C	HOH304
C	HOH307
C	HOH308
C	HOH318
C	HOH329
C	HOH343
C	HOH344
C	HOH349
C	HOH369
C	HOH427
C	HOH490
C	SER17
C	GLY18
C	VAL19
C	GLY20
C	LYS21
C	THR22
C	CYS23
C	PHE33
C	SER39
C	THR40
C	GLY66
C	ASN121
C	LYS122
C	ASP124
C	VAL125
C	SER151

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

Chain	Residue
D	THR22
D	THR40
D	GNP202
D	HOH311
D	HOH314

site_id	AC9
Number of Residues	30
Details	BINDING SITE FOR RESIDUE GNP D 202

Chain	Residue
D	SER17
D	GLY18
D	VAL19
D	GLY20
D	LYS21
D	THR22
D	CYS23
D	PHE33
D	SER39
D	THR40
D	GLY66
D	ASN121
D	LYS122
D	ASP124
D	VAL125
D	SER151
D	ALA152
D	LYS153
D	MG201
D	HOH305
D	HOH308
D	HOH311
D	HOH314
D	HOH335
D	HOH351
D	HOH355
D	HOH376
D	HOH404
D	HOH415
D	HOH482

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

Chain	Residue
E	THR22
E	THR40
E	GNP202
E	HOH304
E	HOH309

site_id	BC2
Number of Residues	31
Details	BINDING SITE FOR RESIDUE GNP E 202

Chain	Residue
E	SER17
E	GLY18
E	VAL19
E	GLY20
E	LYS21
E	THR22
E	CYS23
E	PHE33
E	PHE37
E	SER39
E	THR40
E	GLY66
E	ASN121
E	LYS122
E	ASP124
E	VAL125
E	SER151
E	ALA152
E	LYS153
E	MG201
E	HOH303
E	HOH304
E	HOH308
E	HOH309
E	HOH310
E	HOH331
E	HOH332
E	HOH395
E	HOH407
E	HOH413
E	HOH427

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU11-VAL24

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	70
Details	Motif: {"description":"Switch 1","evidences":[{"source":"UniProtKB","id":"P62820","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	85
Details	Motif: {"description":"Switch 2","evidences":[{"source":"UniProtKB","id":"P62820","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	50
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21378754","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27552051","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3QBT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SZI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27552051","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5SZI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21378754","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27552051","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QBT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SZI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21378754","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3QBT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21378754","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QBT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	5
Details	Modified residue: {"description":"Phosphothreonine; by LRRK2","evidences":[{"source":"PubMed","id":"26824392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29125462","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30209220","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30398148","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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