4I1O

Crystal structure of the Legionella pneumophila GAP domain of LepB in complex with Rab1b bound to GDP and BeF3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003924	molecular_function	GTPase activity
A	0005525	molecular_function	GTP binding
C	0003924	molecular_function	GTPase activity
C	0005525	molecular_function	GTP binding
E	0003924	molecular_function	GTPase activity
E	0005525	molecular_function	GTP binding
G	0003924	molecular_function	GTPase activity
G	0005525	molecular_function	GTP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 201

Chain	Residue
A	SER22
A	THR40
A	ASP63
A	GDP202
A	BEF203
A	HOH306

---

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE GDP A 202

Chain	Residue
A	LYS21
A	SER22
A	CYS23
A	TYR33
A	ILE38
A	ASN121
A	LYS122
A	ASP124
A	LEU125
A	SER151
A	ALA152
A	LYS153
A	MG201
A	BEF203
A	PEG204
A	HOH303
A	HOH306
A	HOH309
D	ARG444
A	GLY18
A	VAL19
A	GLY20

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BEF A 203

Chain	Residue
A	SER17
A	GLY18
A	LYS21
A	SER39
A	THR40
A	GLY66
A	MG201
A	GDP202
D	ARG444

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 204

Chain	Residue
A	TYR33
A	GLU35
A	LYS153
A	GDP202

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 201

Chain	Residue
C	SER22
C	THR40
C	GDP202
C	BEF203
C	HOH304

---

site_id	AC6
Number of Residues	22
Details	BINDING SITE FOR RESIDUE GDP C 202

Chain	Residue
B	ARG444
C	GLY18
C	VAL19
C	GLY20
C	LYS21
C	SER22
C	CYS23
C	TYR33
C	TYR37
C	ASN121
C	LYS122
C	ASP124
C	LEU125
C	SER151
C	ALA152
C	LYS153
C	MG201
C	BEF203
C	PEG204
C	HOH304
C	HOH308
C	HOH312

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BEF C 203

Chain	Residue
B	ARG444
C	SER17
C	GLY18
C	LYS21
C	SER39
C	THR40
C	MG201
C	GDP202

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG C 204

Chain	Residue
C	TYR33
C	GLU35
C	TYR37
C	GDP202

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG C 205

Chain	Residue
B	ASN441
B	LYS482
C	THR40
C	ASP44

---

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG C 206

Chain	Residue
C	LYS10
C	SER76
C	TYR77
C	TYR78
C	ARG79
C	GLY80

---

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG D 701

Chain	Residue
D	LEU562
D	LYS606

---

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

Chain	Residue
E	SER22
E	THR40
E	GDP202
E	BEF203
E	HOH306

---

site_id	BC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE GDP E 202

Chain	Residue
E	GLY20
E	LYS21
E	SER22
E	CYS23
E	TYR33
E	ILE38
E	ASN121
E	LYS122
E	ASP124
E	LEU125
E	SER151
E	ALA152
E	LYS153
E	MG201
E	BEF203
E	HOH306
F	ARG444
F	HOH721
E	GLY18
E	VAL19

---

site_id	BC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE BEF E 203

Chain	Residue
E	SER17
E	GLY18
E	SER22
E	SER39
E	THR40
E	ALA65
E	GLY66
E	MG201
E	GDP202
E	HOH306
F	ARG444

---

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG G 201

Chain	Residue
G	SER22
G	THR40
G	GDP202
G	BEF203
G	HOH307

---

site_id	BC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GDP G 202

Chain	Residue
G	GLY18
G	GLY20
G	LYS21
G	SER22
G	CYS23
G	TYR33
G	TYR37
G	THR40
G	ASN121
G	LYS122
G	ASP124
G	LEU125
G	SER151
G	ALA152
G	LYS153
G	MG201
G	BEF203
G	PEG204
G	HOH307
G	HOH313
H	ARG444

---

site_id	BC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BEF G 203

Chain	Residue
G	SER17
G	GLY18
G	LYS21
G	SER39
G	THR40
G	GLY66
G	MG201
G	GDP202
H	ARG444

---

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG G 204

Chain	Residue
G	GLU35
G	LEU125
G	LYS153
G	GDP202

---

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
A	LEU11-LEU24

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:20064470, ECO:0000269|PubMed:20651120, ECO:0000269|PubMed:23236136, ECO:0000269|PubMed:27552051, ECO:0007744|PDB:3JZA, ECO:0007744|PDB:3NKV, ECO:0007744|PDB:4HLQ, ECO:0007744|PDB:4I1O, ECO:0007744|PDB:5SZH, ECO:0007744|PDB:5SZK

Chain	Residue	Details
A	GLY15
C	GLY15
E	GLY15
G	GLY15

---

site_id	SWS_FT_FI2
Number of Residues	4
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:5SZH, ECO:0007744|PDB:5SZK

Chain	Residue	Details
A	TYR33
C	TYR33
E	TYR33
G	TYR33

---

site_id	SWS_FT_FI3
Number of Residues	4
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
A	ASP63
C	ASP63
E	ASP63
G	ASP63

---

site_id	SWS_FT_FI4
Number of Residues	8
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
A	ASN121
A	SER151
C	ASN121
C	SER151
E	ASN121
E	SER151
G	ASN121
G	SER151

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: (Microbial infection) O-(2-cholinephosphoryl)serine => ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903, ECO:0000269|PubMed:22307087

Chain	Residue	Details
A	SER76
C	SER76
E	SER76
G	SER76

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: (Microbial infection) O-AMP-tyrosine => ECO:0000269|PubMed:20651120

Chain	Residue	Details
A	TYR77
C	TYR77
E	TYR77
G	TYR77

---