Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5O74

Crystal structure of human Rab1b covalently bound to the GEF domain of DrrA/SidM from Legionella pneumophila in the presence of GDP

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0003924	molecular_function	GTPase activity
B	0005525	molecular_function	GTP binding
D	0003924	molecular_function	GTPase activity
D	0005525	molecular_function	GTP binding
F	0003924	molecular_function	GTPase activity
F	0005525	molecular_function	GTP binding
H	0003924	molecular_function	GTPase activity
H	0005525	molecular_function	GTP binding
J	0003924	molecular_function	GTPase activity
J	0005525	molecular_function	GTP binding
L	0003924	molecular_function	GTPase activity
L	0005525	molecular_function	GTP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue GDP B 500

Chain	Residue
B	ASP16
B	ASP124
B	LEU125
B	SER151
B	ALA152
B	LYS153
B	GLY18
B	VAL19
B	GLY20
B	LYS21
B	SER22
B	CYS23
B	ASN121
B	LYS122

site_id	AC2
Number of Residues	15
Details	binding site for residue GDP D 500

Chain	Residue
D	ASP16
D	SER17
D	GLY18
D	VAL19
D	GLY20
D	LYS21
D	SER22
D	CYS23
D	ASN121
D	LYS122
D	ASP124
D	LEU125
D	SER151
D	ALA152
D	LYS153

site_id	AC3
Number of Residues	14
Details	binding site for residue GDP F 500

Chain	Residue
F	ASP16
F	GLY18
F	VAL19
F	GLY20
F	LYS21
F	SER22
F	CYS23
F	ASN121
F	LYS122
F	ASP124
F	LEU125
F	SER151
F	ALA152
F	LYS153

site_id	AC4
Number of Residues	12
Details	binding site for residue GDP H 500

Chain	Residue
H	GLY18
H	VAL19
H	GLY20
H	LYS21
H	SER22
H	CYS23
H	ASN121
H	LYS122
H	ASP124
H	SER151
H	ALA152
H	LYS153

site_id	AC5
Number of Residues	12
Details	binding site for residue GDP J 500

Chain	Residue
J	ASP16
J	GLY18
J	VAL19
J	GLY20
J	LYS21
J	SER22
J	CYS23
J	ASN121
J	LYS122
J	SER151
J	ALA152
J	LYS153

site_id	AC6
Number of Residues	15
Details	binding site for residue GDP L 500

Chain	Residue
L	ASP16
L	SER17
L	GLY18
L	VAL19
L	GLY20
L	LYS21
L	SER22
L	CYS23
L	ASN121
L	LYS122
L	ASP124
L	LEU125
L	SER151
L	ALA152
L	LYS153

site_id	AC7
Number of Residues	6
Details	binding site for Di-peptide TYR D 78 and 9MN D 79

Chain	Residue
C	ARG418
C	CYS512
D	ILE14
D	GLY80
D	ALA81
K	ASP459

site_id	AC8
Number of Residues	10
Details	binding site for Di-peptide 9MN D 79 and CYS C 512

Chain	Residue
C	ARG418
C	ASN511
C	GLU513
C	THR514
C	LEU515
C	GLU516
D	TYR78
D	GLY80
D	ALA81
K	ASP459

site_id	AC9
Number of Residues	5
Details	binding site for Di-peptide 9MN D 79 and GLY D 80

Chain	Residue
C	CYS512
D	TYR78
D	ALA81
K	ASP459
C	ARG418

site_id	AD1
Number of Residues	10
Details	binding site for Di-peptide TYR F 78 and 9MN F 79

Chain	Residue
E	ARG418
E	CYS512
E	GLU513
F	THR74
F	SER75
F	SER76
F	TYR77
F	GLY80
F	ALA81
F	TYR109

site_id	AD2
Number of Residues	10
Details	binding site for Di-peptide 9MN F 79 and CYS E 512

Chain	Residue
E	ARG418
E	ASN511
E	GLU513
E	THR514
E	LEU515
E	GLU516
F	SER75
F	TYR78
F	GLY80
F	ALA81

site_id	AD3
Number of Residues	6
Details	binding site for Di-peptide 9MN F 79 and GLY F 80

Chain	Residue
E	ARG418
E	CYS512
E	GLU513
F	SER75
F	TYR78
F	ALA81

site_id	AD4
Number of Residues	9
Details	binding site for Di-peptide TYR H 78 and 9MN H 79

Chain	Residue
G	ARG418
G	CYS512
H	THR74
H	SER75
H	SER76
H	TYR77
H	GLY80
H	ALA81
H	TYR109

site_id	AD5
Number of Residues	5
Details	binding site for Di-peptide 9MN H 79 and GLY H 80

Chain	Residue
G	ARG418
G	CYS512
H	SER75
H	TYR78
H	ALA81

site_id	AD6
Number of Residues	10
Details	binding site for Di-peptide 9MN H 79 and CYS G 512

Chain	Residue
G	ARG418
G	ASN511
G	GLU513
G	THR514
G	LEU515
G	GLU516
H	SER75
H	TYR78
H	GLY80
H	ALA81

site_id	AD7
Number of Residues	9
Details	binding site for Di-peptide TYR J 78 and 9MN J 79

Chain	Residue
I	ARG418
I	CYS512
J	THR74
J	SER75
J	SER76
J	TYR77
J	GLY80
J	ALA81
J	TYR109

site_id	AD8
Number of Residues	5
Details	binding site for Di-peptide 9MN J 79 and GLY J 80

Chain	Residue
I	ARG418
I	CYS512
J	SER75
J	TYR78
J	ALA81

site_id	AD9
Number of Residues	10
Details	binding site for Di-peptide 9MN J 79 and CYS I 512

Chain	Residue
I	ARG418
I	ASN511
I	GLU513
I	THR514
I	LEU515
I	GLU516
J	SER75
J	TYR78
J	GLY80
J	ALA81

site_id	AE1
Number of Residues	6
Details	binding site for Di-peptide TYR L 78 and 9MN L 79

Chain	Residue
K	ASP415
K	ARG418
K	CYS512
L	GLY80
L	ALA81
L	ILE106

site_id	AE2
Number of Residues	6
Details	binding site for Di-peptide 9MN L 79 and GLY L 80

Chain	Residue
K	ASP415
K	ARG418
K	CYS512
L	LYS10
L	TYR78
L	ALA81

site_id	AE3
Number of Residues	10
Details	binding site for Di-peptide 9MN L 79 and CYS K 512

Chain	Residue
K	ASP415
K	ARG418
K	ASN511
K	GLU513
K	THR514
K	LEU515
K	GLU516
L	TYR78
L	GLY80
L	ALA81

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. LLLiGDSGVGKscL

Chain	Residue	Details
B	LEU11-LEU24

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	60
Details	BINDING: BINDING => ECO:0000269\|PubMed:20651120, ECO:0000269\|PubMed:27552051, ECO:0007744\|PDB:3NKV, ECO:0007744\|PDB:5SZH, ECO:0007744\|PDB:5SZK

Chain	Residue	Details
B	SER17
B	LYS153
D	SER17
D	GLY20
D	LYS21
D	CYS23
D	GLU35
D	GLY66
D	ASN121
D	ASP124
D	ALA152
B	GLY20
D	LYS153
F	SER17
F	GLY20
F	LYS21
F	CYS23
F	GLU35
F	GLY66
F	ASN121
F	ASP124
F	ALA152
B	LYS21
F	LYS153
H	SER17
H	GLY20
H	LYS21
H	CYS23
H	GLU35
H	GLY66
H	ASN121
H	ASP124
H	ALA152
B	CYS23
H	LYS153
J	SER17
J	GLY20
J	LYS21
J	CYS23
J	GLU35
J	GLY66
J	ASN121
J	ASP124
J	ALA152
B	GLU35
J	LYS153
L	SER17
L	GLY20
L	LYS21
L	CYS23
L	GLU35
L	GLY66
L	ASN121
L	ASP124
L	ALA152
B	GLY66
L	LYS153
B	ASN121
B	ASP124
B	ALA152

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:27552051, ECO:0007744\|PDB:5SZH, ECO:0007744\|PDB:5SZK

Chain	Residue	Details
B	GLY18
J	LYS122
L	GLY18
L	LYS122
B	LYS122
D	GLY18
D	LYS122
F	GLY18
F	LYS122
H	GLY18
H	LYS122
J	GLY18

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0007744\|PDB:3NKV

Chain	Residue	Details
B	VAL19
D	VAL19
F	VAL19
H	VAL19
J	VAL19
L	VAL19

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:20651120, ECO:0000269\|PubMed:23236136, ECO:0000269\|PubMed:27552051, ECO:0007744\|PDB:3NKV, ECO:0007744\|PDB:4HLQ, ECO:0007744\|PDB:4I1O, ECO:0007744\|PDB:5SZH, ECO:0007744\|PDB:5SZK

Chain	Residue	Details
B	SER22
J	THR40
L	SER22
L	THR40
B	THR40
D	SER22
D	THR40
F	SER22
F	THR40
H	SER22
H	THR40
J	SER22

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:27552051, ECO:0007744\|PDB:5SZH

Chain	Residue	Details
B	TYR33
J	SER39
L	TYR33
L	SER39
B	SER39
D	TYR33
D	SER39
F	TYR33
F	SER39
H	TYR33
H	SER39
J	TYR33

site_id	SWS_FT_FI6
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:20651120, ECO:0007744\|PDB:3NKV

Chain	Residue	Details
B	THR34
J	SER36
L	THR34
L	SER36
B	SER36
D	THR34
D	SER36
F	THR34
F	SER36
H	THR34
H	SER36
J	THR34

site_id	SWS_FT_FI7
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:23236136, ECO:0000269\|PubMed:27552051, ECO:0007744\|PDB:4HLQ, ECO:0007744\|PDB:5SZH

Chain	Residue	Details
B	ASP63
D	ASP63
F	ASP63
H	ASP63
J	ASP63
L	ASP63

site_id	SWS_FT_FI8
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:27552051, ECO:0007744\|PDB:5SZK

Chain	Residue	Details
B	SER151
D	SER151
F	SER151
H	SER151
J	SER151
L	SER151

site_id	SWS_FT_FI9
Number of Residues	6
Details	MOD_RES: N-acetylmethionine => ECO:0000269\|Ref.5

Chain	Residue	Details
B	MET1
D	MET1
F	MET1
H	MET1
J	MET1
L	MET1

site_id	SWS_FT_FI10
Number of Residues	6
Details	MOD_RES: (Microbial infection) O-(2-cholinephosphoryl)serine => ECO:0000269\|PubMed:21822290, ECO:0000269\|PubMed:22158903, ECO:0000269\|PubMed:22307087

Chain	Residue	Details
B	SER76
D	SER76
F	SER76
H	SER76
J	SER76
L	SER76

site_id	SWS_FT_FI11
Number of Residues	6
Details	MOD_RES: (Microbial infection) O-AMP-tyrosine => ECO:0000269\|PubMed:20651120

Chain	Residue	Details
B	TYR77
D	TYR77
F	TYR77
H	TYR77
J	TYR77
L	TYR77

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