Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5F2Q

C-type lectin from Bothrops jararacussu

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0030246	molecular_function	carbohydrate binding
A	0030308	biological_process	negative regulation of cell growth
A	0038023	molecular_function	signaling receptor activity
A	0046872	molecular_function	metal ion binding
B	0005576	cellular_component	extracellular region
B	0030246	molecular_function	carbohydrate binding
B	0030308	biological_process	negative regulation of cell growth
B	0038023	molecular_function	signaling receptor activity
B	0046872	molecular_function	metal ion binding
C	0005576	cellular_component	extracellular region
C	0030246	molecular_function	carbohydrate binding
C	0030308	biological_process	negative regulation of cell growth
C	0038023	molecular_function	signaling receptor activity
C	0046872	molecular_function	metal ion binding
D	0005576	cellular_component	extracellular region
D	0030246	molecular_function	carbohydrate binding
D	0030308	biological_process	negative regulation of cell growth
D	0038023	molecular_function	signaling receptor activity
D	0046872	molecular_function	metal ion binding
E	0005576	cellular_component	extracellular region
E	0030246	molecular_function	carbohydrate binding
E	0030308	biological_process	negative regulation of cell growth
E	0038023	molecular_function	signaling receptor activity
E	0046872	molecular_function	metal ion binding
F	0005576	cellular_component	extracellular region
F	0030246	molecular_function	carbohydrate binding
F	0030308	biological_process	negative regulation of cell growth
F	0038023	molecular_function	signaling receptor activity
F	0046872	molecular_function	metal ion binding
G	0005576	cellular_component	extracellular region
G	0030246	molecular_function	carbohydrate binding
G	0030308	biological_process	negative regulation of cell growth
G	0038023	molecular_function	signaling receptor activity
G	0046872	molecular_function	metal ion binding
H	0005576	cellular_component	extracellular region
H	0030246	molecular_function	carbohydrate binding
H	0030308	biological_process	negative regulation of cell growth
H	0038023	molecular_function	signaling receptor activity
H	0046872	molecular_function	metal ion binding
I	0005576	cellular_component	extracellular region
I	0030246	molecular_function	carbohydrate binding
I	0030308	biological_process	negative regulation of cell growth
I	0038023	molecular_function	signaling receptor activity
I	0046872	molecular_function	metal ion binding
J	0005576	cellular_component	extracellular region
J	0030246	molecular_function	carbohydrate binding
J	0030308	biological_process	negative regulation of cell growth
J	0038023	molecular_function	signaling receptor activity
J	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue CA A 201

Chain	Residue
A	GLN96
A	ASP98
A	GLU104
A	ASN119
A	ASP120
A	HOH301
A	HOH302

site_id	AC2
Number of Residues	4
Details	binding site for residue NA A 202

Chain	Residue
A	HIS44
A	GLN132
A	TYR15
A	SER42

site_id	AC3
Number of Residues	6
Details	binding site for residue CA B 201

Chain	Residue
B	GLN96
B	ASP98
B	GLU104
B	ASN119
B	ASP120
B	HOH301

site_id	AC4
Number of Residues	5
Details	binding site for residue NA B 202

Chain	Residue
B	LEU13
B	TYR15
B	SER42
B	HIS44
B	GLN132

site_id	AC5
Number of Residues	5
Details	binding site for residue CA C 201

Chain	Residue
C	GLN96
C	ASP98
C	GLU104
C	ASN119
C	ASP120

site_id	AC6
Number of Residues	4
Details	binding site for residue NA C 202

Chain	Residue
C	TYR15
C	SER42
C	HIS44
C	GLN132

site_id	AC7
Number of Residues	6
Details	binding site for residue CA D 201

Chain	Residue
D	GLN96
D	ASP98
D	GLU104
D	ASN119
D	ASP120
D	HOH301

site_id	AC8
Number of Residues	4
Details	binding site for residue NA D 202

Chain	Residue
D	LEU13
D	TYR15
D	SER42
D	GLN132

site_id	AC9
Number of Residues	6
Details	binding site for residue CA E 201

Chain	Residue
E	GLN96
E	ASP98
E	GLU104
E	ASN119
E	ASP120
E	HOH305

site_id	AD1
Number of Residues	6
Details	binding site for residue NA E 202

Chain	Residue
E	LEU13
E	TYR15
E	SER42
E	GLN132
E	HOH301
E	HOH309

site_id	AD2
Number of Residues	6
Details	binding site for residue CA F 201

Chain	Residue
F	GLN96
F	ASP98
F	GLU104
F	ASN119
F	ASP120
F	HOH302

site_id	AD3
Number of Residues	4
Details	binding site for residue NA F 202

Chain	Residue
F	TYR15
F	SER42
F	GLN132
F	HOH301

site_id	AD4
Number of Residues	6
Details	binding site for residue CA G 201

Chain	Residue
G	GLN96
G	ASP98
G	GLU104
G	ASN119
G	ASP120
G	HOH302

site_id	AD5
Number of Residues	4
Details	binding site for residue NA G 202

Chain	Residue
G	TYR15
G	SER42
G	GLN132
G	HOH301

site_id	AD6
Number of Residues	6
Details	binding site for residue CA H 201

Chain	Residue
H	GLN96
H	ASP98
H	GLU104
H	ASN119
H	ASP120
H	HOH301

site_id	AD7
Number of Residues	4
Details	binding site for residue NA H 202

Chain	Residue
H	TYR15
H	SER42
H	HIS44
H	GLN132

site_id	AD8
Number of Residues	6
Details	binding site for residue CA I 201

Chain	Residue
I	GLN96
I	ASP98
I	GLU104
I	ASN119
I	ASP120
I	HOH301

site_id	AD9
Number of Residues	5
Details	binding site for residue NA I 202

Chain	Residue
I	LEU13
I	TYR15
I	SER42
I	HIS44
I	GLN132

site_id	AE1
Number of Residues	7
Details	binding site for residue CA J 201

Chain	Residue
J	HOH301
J	HOH302
J	GLN96
J	ASP98
J	GLU104
J	ASN119
J	ASP120

site_id	AE2
Number of Residues	5
Details	binding site for residue NA J 202

Chain	Residue
J	LEU13
J	TYR15
J	SER42
J	HIS44
J	GLN132

Functional Information from PROSITE/UniProt

site_id	PS00615
Number of Residues	26
Details	C_TYPE_LECTIN_1 C-type lectin domain signature. CVelvsntgyrl..WNDQVCeskna.FLC

Chain	Residue	Details
A	CYS106-CYS131

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	50
Details	BINDING: BINDING => ECO:0000269\|PubMed:28003128, ECO:0007744\|PDB:5F2Q

Chain	Residue	Details
A	GLN96
A	ASP98
A	GLU104
A	ASN119
A	ASP120
B	GLN96
B	ASP98
B	GLU104
B	ASN119
B	ASP120
C	GLN96
C	ASP98
C	GLU104
C	ASN119
C	ASP120
D	GLN96
D	ASP98
D	GLU104
D	ASN119
D	ASP120
E	GLN96
E	ASP98
E	GLU104
E	ASN119
E	ASP120
F	GLN96
F	ASP98
F	GLU104
F	ASN119
F	ASP120
G	GLN96
G	ASP98
G	GLU104
G	ASN119
G	ASP120
H	GLN96
H	ASP98
H	GLU104
H	ASN119
H	ASP120
I	GLN96
I	ASP98
I	GLU104
I	ASN119
I	ASP120
J	GLN96
J	ASP98
J	GLU104
J	ASN119
J	ASP120

site_id	SWS_FT_FI2
Number of Residues	10
Details	SITE: Binds aminoglycoside antibiotics (subunit E') => ECO:0000269\|PubMed:28003128

Chain	Residue	Details
B	TRP79
A	TRP79
C	TRP79
D	TRP79
E	TRP79
F	TRP79
G	TRP79
H	TRP79
I	TRP79
J	TRP79

site_id	SWS_FT_FI3
Number of Residues	20
Details	SITE: Binds aminoglycoside antibiotics (subunit A and E') => ECO:0000269\|PubMed:28003128

Chain	Residue	Details
A	GLU80
A	THR87
B	GLU80
B	THR87
C	GLU80
C	THR87
D	GLU80
D	THR87
E	GLU80
E	THR87
F	GLU80
F	THR87
G	GLU80
G	THR87
H	GLU80
H	THR87
I	GLU80
I	THR87
J	GLU80
J	THR87

site_id	SWS_FT_FI4
Number of Residues	20
Details	SITE: Binds aminoglycoside antibiotics (subunit A) => ECO:0000269\|PubMed:28003128

Chain	Residue	Details
A	TRP81
A	SER85
B	TRP81
B	SER85
C	TRP81
C	SER85
D	TRP81
D	SER85
E	TRP81
E	SER85
F	TRP81
F	SER85
G	TRP81
G	SER85
H	TRP81
H	SER85
I	TRP81
I	SER85
J	TRP81
J	SER85

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