Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4M3C

Structure of a binary complex between homologous tetrameric legume lectins from Butea monosperma and Spatholobus parviflorus seeds

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0030246	molecular_function	carbohydrate binding
A	0046872	molecular_function	metal ion binding
B	0030246	molecular_function	carbohydrate binding
B	0046872	molecular_function	metal ion binding
C	0030246	molecular_function	carbohydrate binding
C	0046872	molecular_function	metal ion binding
D	0030246	molecular_function	carbohydrate binding
D	0046872	molecular_function	metal ion binding
E	0005509	molecular_function	calcium ion binding
E	0005515	molecular_function	protein binding
E	0005534	molecular_function	galactose binding
E	0015066	molecular_function	alpha-amylase inhibitor activity
E	0030145	molecular_function	manganese ion binding
E	0030246	molecular_function	carbohydrate binding
E	0030395	molecular_function	lactose binding
E	0031640	biological_process	killing of cells of another organism
E	0032991	cellular_component	protein-containing complex
E	0046872	molecular_function	metal ion binding
E	0050832	biological_process	defense response to fungus
F	0005509	molecular_function	calcium ion binding
F	0005515	molecular_function	protein binding
F	0005534	molecular_function	galactose binding
F	0015066	molecular_function	alpha-amylase inhibitor activity
F	0030145	molecular_function	manganese ion binding
F	0030246	molecular_function	carbohydrate binding
F	0030395	molecular_function	lactose binding
F	0031640	biological_process	killing of cells of another organism
F	0032991	cellular_component	protein-containing complex
F	0046872	molecular_function	metal ion binding
F	0050832	biological_process	defense response to fungus
G	0005509	molecular_function	calcium ion binding
G	0005515	molecular_function	protein binding
G	0005534	molecular_function	galactose binding
G	0015066	molecular_function	alpha-amylase inhibitor activity
G	0030145	molecular_function	manganese ion binding
G	0030246	molecular_function	carbohydrate binding
G	0030395	molecular_function	lactose binding
G	0031640	biological_process	killing of cells of another organism
G	0032991	cellular_component	protein-containing complex
G	0046872	molecular_function	metal ion binding
G	0050832	biological_process	defense response to fungus
H	0005509	molecular_function	calcium ion binding
H	0005515	molecular_function	protein binding
H	0005534	molecular_function	galactose binding
H	0015066	molecular_function	alpha-amylase inhibitor activity
H	0030145	molecular_function	manganese ion binding
H	0030246	molecular_function	carbohydrate binding
H	0030395	molecular_function	lactose binding
H	0031640	biological_process	killing of cells of another organism
H	0032991	cellular_component	protein-containing complex
H	0046872	molecular_function	metal ion binding
H	0050832	biological_process	defense response to fungus

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 301

Chain	Residue
A	ASP128
A	TYR130
A	ASN132
A	ASP137
A	HOH421
A	HOH426

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 302

Chain	Residue
A	HIS142
A	HOH401
A	HOH422
A	GLU126
A	ASP128
A	ASP137

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ABU A 303

Chain	Residue
A	ASN2
A	THR3
A	ASP4
A	ILE57
A	ASN58
A	SER235
D	THR7
D	PHE8
D	ASN17

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 301

Chain	Residue
B	ASP128
B	TYR130
B	ASN132
B	ASP137
B	HOH430
B	HOH434

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN B 302

Chain	Residue
B	GLU126
B	ASP128
B	ASP137
B	HIS142
B	HOH420
B	HOH435

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ABU B 303

Chain	Residue
B	ASN2
B	ASP4
B	ILE57
B	ASN58
B	TRP207
B	SER235
B	LYS236
B	HOH408
C	ASN17

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 301

Chain	Residue
C	ASP128
C	TYR130
C	ASN132
C	ASP137
C	HOH423
C	HOH430

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN C 302

Chain	Residue
C	GLU126
C	ASP128
C	ASP137
C	HIS142
C	HOH407
C	HOH423
C	HOH429

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ABU C 303

Chain	Residue
B	ASN17
B	HOH403
B	HOH436
C	ASN2
C	ASP4
C	ILE57
C	ASN58
C	TRP207
C	SER235
C	HOH426

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 304

Chain	Residue
C	LEU52
C	TYR53
C	ALA54
C	VAL97
C	SER98
C	SER209

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 301

Chain	Residue
D	ASP128
D	TYR130
D	ASN132
D	ASP137
D	HOH413
D	HOH420

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 302

Chain	Residue
D	GLU126
D	ASP128
D	ASP137
D	HIS142
D	HOH425

site_id	BC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ABU D 303

Chain	Residue
A	THR7
A	PHE8
A	LYS12
A	GLN15
A	ASN17
D	ASN2
D	THR3
D	ASP4
D	ASN58
D	TRP207
D	HOH409

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL D 304

Chain	Residue
C	THR171
C	VAL180
D	HOH430

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 301

Chain	Residue
E	ASP137
E	HOH411
E	HOH430
E	ASP128
E	TYR130
E	ASN132

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN E 302

Chain	Residue
E	GLU126
E	ASP128
E	ASP137
E	HIS142
E	HOH426
E	HOH428

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ABU E 303

Chain	Residue
E	PRO205
E	GLU206
E	TRP207

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA F 301

Chain	Residue
F	ASP128
F	TYR130
F	ASN132
F	ASP137
F	HOH411
F	HOH426

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN F 302

Chain	Residue
F	GLU126
F	ASP128
F	ASP137
F	HIS142
F	HOH415
F	HOH430

site_id	CC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL F 303

Chain	Residue
F	HOH428

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA G 301

Chain	Residue
G	ASP128
G	TYR130
G	ASN132
G	ASP137
G	HOH431
G	HOH434

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN G 302

Chain	Residue
G	GLU126
G	ASP128
G	ASP137
G	HIS142
G	HOH432
G	HOH433

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA H 301

Chain	Residue
H	ASP128
H	TYR130
H	ASN132
H	ASP137
H	HOH406
H	HOH411

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN H 302

Chain	Residue
H	GLU126
H	ASP128
H	ASP137
H	HIS142
H	HOH433

site_id	CC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ABU H 303

Chain	Residue
E	VAL7
E	ASN17
H	GLU2
H	GLU3
H	THR4
H	ILE57
H	ASN58
H	TRP207
H	SER235
H	HOH404
H	HOH414

Functional Information from PROSITE/UniProt

site_id	PS00092
Number of Residues	7
Details	N6_MTASE N-6 Adenine-specific DNA methylases signature. VFTDPPY

Chain	Residue	Details
E	VAL134-TYR140
F	VAL134-TYR140

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

Chain	Residue	Details
B	VAL123-THR129
E	VAL123-THR129
F	VAL123-THR129
A	VAL123-THR129

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

Chain	Residue	Details
B	LEU204-SER213
E	LEU204-SER213
F	LEU204-SER213
A	LEU204-SER213

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI5
Number of Residues	26
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P02870","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21889532","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3IPV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4M3C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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