Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1VLN

A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005537	molecular_function	D-mannose binding
A	0030246	molecular_function	carbohydrate binding
A	0035821	biological_process	modulation of process of another organism
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0090729	molecular_function	toxin activity
B	0005537	molecular_function	D-mannose binding
B	0030246	molecular_function	carbohydrate binding
B	0035821	biological_process	modulation of process of another organism
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0090729	molecular_function	toxin activity
C	0005537	molecular_function	D-mannose binding
C	0030246	molecular_function	carbohydrate binding
C	0035821	biological_process	modulation of process of another organism
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0090729	molecular_function	toxin activity
D	0005537	molecular_function	D-mannose binding
D	0030246	molecular_function	carbohydrate binding
D	0035821	biological_process	modulation of process of another organism
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0090729	molecular_function	toxin activity
E	0005537	molecular_function	D-mannose binding
E	0030246	molecular_function	carbohydrate binding
E	0035821	biological_process	modulation of process of another organism
E	0042802	molecular_function	identical protein binding
E	0046872	molecular_function	metal ion binding
E	0090729	molecular_function	toxin activity
F	0005537	molecular_function	D-mannose binding
F	0030246	molecular_function	carbohydrate binding
F	0035821	biological_process	modulation of process of another organism
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding
F	0090729	molecular_function	toxin activity
G	0005537	molecular_function	D-mannose binding
G	0030246	molecular_function	carbohydrate binding
G	0035821	biological_process	modulation of process of another organism
G	0042802	molecular_function	identical protein binding
G	0046872	molecular_function	metal ion binding
G	0090729	molecular_function	toxin activity
H	0005537	molecular_function	D-mannose binding
H	0030246	molecular_function	carbohydrate binding
H	0035821	biological_process	modulation of process of another organism
H	0042802	molecular_function	identical protein binding
H	0046872	molecular_function	metal ion binding
H	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 238

Chain	Residue
A	GLU8
A	ASP10
A	ASP19
A	HIS24
A	HOH240
A	HOH241

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 239

Chain	Residue
A	ASP19
A	HOH242
A	HOH243
A	ASP10
A	TYR12
A	ASN14

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN B 238

Chain	Residue
B	GLU8
B	ASP10
B	ASP19
B	HIS24
B	HOH240
B	HOH241

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 239

Chain	Residue
B	ASP10
B	TYR12
B	ASN14
B	ASP19
B	HOH242
B	HOH243

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 238

Chain	Residue
C	GLU8
C	ASP10
C	ASP19
C	HIS24
C	HOH240

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 239

Chain	Residue
C	ASP10
C	TYR12
C	ASN14
C	ASP19
C	HOH242
C	HOH243

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN D 238

Chain	Residue
D	GLU8
D	ASP10
D	ASP19
D	HIS24
D	HOH240
D	HOH241

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 239

Chain	Residue
D	ASP10
D	TYR12
D	ASN14
D	ASP19
D	HOH242
D	HOH243

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN E 238

Chain	Residue
E	GLU8
E	ASP10
E	ASP19
E	HIS24
E	HOH240
E	HOH241

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 239

Chain	Residue
E	ASP10
E	TYR12
E	ASN14
E	ASP19
E	HOH242
E	HOH243

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN F 238

Chain	Residue
F	GLU8
F	ASP10
F	ASP19
F	HIS24
F	HOH240
F	HOH241

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA F 239

Chain	Residue
F	ASP10
F	TYR12
F	ASN14
F	ASP19
F	HOH242
F	HOH243

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN G 238

Chain	Residue
G	GLU8
G	ASP10
G	ASP19
G	HIS24
G	HOH240
G	HOH241

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA G 239

Chain	Residue
G	ASP10
G	TYR12
G	ASN14
G	ASP19
G	HOH242
G	HOH243

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN H 238

Chain	Residue
H	GLU8
H	ASP10
H	ASP19
H	HIS24
H	HOH240
H	HOH241

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA H 239

Chain	Residue
H	ASP10
H	TYR12
H	ASN14
H	ASP19
H	HOH242
H	HOH243

Functional Information from PROSITE/UniProt

site_id	PS00307
Number of Residues	7
Details	LECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVELDT

Chain	Residue	Details
A	VAL5-THR11

site_id	PS00308
Number of Residues	10
Details	LECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. LPEWVRVGLS

Chain	Residue	Details
A	LEU85-SER94

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8812975","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9830028","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details