Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4WMO

Selenomethionine derivative of Xenopus laevis embryonic epidermal lectin carbohydrate-binding domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0030133	cellular_component	transport vesicle
A	0030141	cellular_component	secretory granule
A	0030246	molecular_function	carbohydrate binding
A	0031410	cellular_component	cytoplasmic vesicle
A	0034214	biological_process	protein hexamerization
A	0046872	molecular_function	metal ion binding
A	0070492	molecular_function	oligosaccharide binding
B	0005509	molecular_function	calcium ion binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0030133	cellular_component	transport vesicle
B	0030141	cellular_component	secretory granule
B	0030246	molecular_function	carbohydrate binding
B	0031410	cellular_component	cytoplasmic vesicle
B	0034214	biological_process	protein hexamerization
B	0046872	molecular_function	metal ion binding
B	0070492	molecular_function	oligosaccharide binding
C	0005509	molecular_function	calcium ion binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0030133	cellular_component	transport vesicle
C	0030141	cellular_component	secretory granule
C	0030246	molecular_function	carbohydrate binding
C	0031410	cellular_component	cytoplasmic vesicle
C	0034214	biological_process	protein hexamerization
C	0046872	molecular_function	metal ion binding
C	0070492	molecular_function	oligosaccharide binding
D	0005509	molecular_function	calcium ion binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0030133	cellular_component	transport vesicle
D	0030141	cellular_component	secretory granule
D	0030246	molecular_function	carbohydrate binding
D	0031410	cellular_component	cytoplasmic vesicle
D	0034214	biological_process	protein hexamerization
D	0046872	molecular_function	metal ion binding
D	0070492	molecular_function	oligosaccharide binding
E	0005509	molecular_function	calcium ion binding
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0030133	cellular_component	transport vesicle
E	0030141	cellular_component	secretory granule
E	0030246	molecular_function	carbohydrate binding
E	0031410	cellular_component	cytoplasmic vesicle
E	0034214	biological_process	protein hexamerization
E	0046872	molecular_function	metal ion binding
E	0070492	molecular_function	oligosaccharide binding
F	0005509	molecular_function	calcium ion binding
F	0005576	cellular_component	extracellular region
F	0005615	cellular_component	extracellular space
F	0030133	cellular_component	transport vesicle
F	0030141	cellular_component	secretory granule
F	0030246	molecular_function	carbohydrate binding
F	0031410	cellular_component	cytoplasmic vesicle
F	0034214	biological_process	protein hexamerization
F	0046872	molecular_function	metal ion binding
F	0070492	molecular_function	oligosaccharide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue CA F 401

Chain	Residue
F	ASN289
F	GLU291
F	GLU303
F	HOH527
F	HOH556
F	HOH568
F	HOH686

site_id	AC2
Number of Residues	6
Details	binding site for residue CA F 402

Chain	Residue
F	ASP162
F	ASP311
F	HOH619
F	HOH687
F	HIS115
F	GLY126

site_id	AC3
Number of Residues	6
Details	binding site for residue CA F 403

Chain	Residue
F	GLU116
F	ASN118
F	GLY121
F	ASP127
F	HOH536
F	HOH618

site_id	AC4
Number of Residues	5
Details	binding site for residue 1PE F 404

Chain	Residue
F	GLU141
F	LYS222
F	ASP224
F	ILE225
F	HOH574

site_id	AC5
Number of Residues	4
Details	binding site for residue 1PE F 405

Chain	Residue
F	SER258
F	PHE260
F	THR261
F	LYS286

site_id	AC6
Number of Residues	7
Details	binding site for residue CA C 401

Chain	Residue
C	ASN289
C	GLU291
C	GLU303
C	HOH557
C	HOH565
C	HOH650
C	HOH653

site_id	AC7
Number of Residues	6
Details	binding site for residue CA C 402

Chain	Residue
C	GLU116
C	ASN118
C	GLY121
C	ASP127
C	HOH550
C	HOH620

site_id	AC8
Number of Residues	6
Details	binding site for residue CA C 403

Chain	Residue
C	HIS115
C	GLY126
C	ASP162
C	ASP311
C	HOH558
C	HOH723

site_id	AC9
Number of Residues	4
Details	binding site for residue 1PE C 404

Chain	Residue
C	GLU141
C	LYS222
C	ASP224
C	ILE225

site_id	AD1
Number of Residues	4
Details	binding site for residue 1PE C 405

Chain	Residue
C	SER258
C	THR261
C	LYS284
C	LYS286

site_id	AD2
Number of Residues	2
Details	binding site for residue 1PE C 406

Chain	Residue
C	LYS227
C	CYS228

site_id	AD3
Number of Residues	7
Details	binding site for residue CA B 401

Chain	Residue
B	ASN289
B	GLU291
B	GLU303
B	HOH504
B	HOH512
B	HOH544
B	HOH551

site_id	AD4
Number of Residues	6
Details	binding site for residue CA B 402

Chain	Residue
B	GLU116
B	ASN118
B	GLY121
B	ASP127
B	HOH538
B	HOH732

site_id	AD5
Number of Residues	6
Details	binding site for residue CA B 403

Chain	Residue
B	HIS115
B	GLY126
B	ASP162
B	ASP311
B	HOH566
B	HOH733

site_id	AD6
Number of Residues	6
Details	binding site for residue 1PE B 404

Chain	Residue
B	GLU141
B	LYS222
B	TYR223
B	ASP224
B	HOH647
B	HOH721

site_id	AD7
Number of Residues	2
Details	binding site for residue 1PE B 405

Chain	Residue
B	CYS228
B	LYS286

site_id	AD8
Number of Residues	6
Details	binding site for residue CA D 401

Chain	Residue
D	ASN289
D	GLU291
D	GLU303
D	HOH593
D	HOH680
D	HOH710

site_id	AD9
Number of Residues	6
Details	binding site for residue CA D 402

Chain	Residue
D	HIS115
D	GLY126
D	ASP162
D	ASP311
D	HOH534
D	HOH586

site_id	AE1
Number of Residues	6
Details	binding site for residue CA D 403

Chain	Residue
D	ASP127
D	HOH554
D	HOH560
D	GLU116
D	ASN118
D	GLY121

site_id	AE2
Number of Residues	4
Details	binding site for residue 1PE D 404

Chain	Residue
D	GLU141
D	LYS222
D	ASP224
D	ILE225

site_id	AE3
Number of Residues	6
Details	binding site for residue 1PE D 405

Chain	Residue
D	SER258
D	PHE260
D	THR261
D	LYS284
D	LYS286
D	HOH511

site_id	AE4
Number of Residues	7
Details	binding site for residue CA E 401

Chain	Residue
E	ASN289
E	GLU291
E	GLU303
E	HOH540
E	HOH549
E	HOH556
E	HOH715

site_id	AE5
Number of Residues	6
Details	binding site for residue CA E 402

Chain	Residue
E	HIS115
E	GLY126
E	ASP162
E	ASP311
E	HOH526
E	HOH736

site_id	AE6
Number of Residues	6
Details	binding site for residue CA E 403

Chain	Residue
E	GLU116
E	ASN118
E	GLY121
E	ASP127
E	HOH532
E	HOH735

site_id	AE7
Number of Residues	3
Details	binding site for residue 1PE E 404

Chain	Residue
E	GLU141
E	LYS222
E	ILE225

site_id	AE8
Number of Residues	6
Details	binding site for residue 1PE E 405

Chain	Residue
E	SER258
E	PHE260
E	THR261
E	LYS284
E	LYS286
E	HOH504

site_id	AE9
Number of Residues	7
Details	binding site for residue CA A 401

Chain	Residue
A	ASN289
A	GLU291
A	GLU303
A	HOH550
A	HOH566
A	HOH577
A	HOH735

site_id	AF1
Number of Residues	6
Details	binding site for residue CA A 402

Chain	Residue
A	HIS115
A	GLY126
A	ASP162
A	ASP311
A	HOH764
A	HOH765

site_id	AF2
Number of Residues	6
Details	binding site for residue CA A 403

Chain	Residue
A	GLU116
A	ASN118
A	GLY121
A	ASP127
A	HOH549
A	HOH733

site_id	AF3
Number of Residues	5
Details	binding site for residue 1PE A 404

Chain	Residue
A	GLU141
A	LYS222
A	ASP224
A	ILE225
A	HOH629

site_id	AF4
Number of Residues	5
Details	binding site for residue 1PE A 405

Chain	Residue
A	SER258
A	PHE260
A	THR261
A	LYS284
A	LYS286

site_id	AF5
Number of Residues	2
Details	binding site for residue 1PE A 406

Chain	Residue
A	CYS228
A	LYS286

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	66
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26755729","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WN0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26755729","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15537792","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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