Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5ZC0

Crystal structure of Xenopus embryonic epidermal lectin in complex with Samarium ions

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	6
Details	binding site for residue CA A 401

Chain	Residue
A	GLU116
A	ASN118
A	GLY121
A	ASP127
A	HOH508
A	HOH525

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

Chain	Residue
A	ASP311
A	HOH501
A	HOH530
A	HIS115
A	GLY126
A	ASP162

site_id	AC3
Number of Residues	7
Details	binding site for residue SM A 403

Chain	Residue
A	ASN289
A	GLU291
A	GLU303
A	HOH503
A	HOH521
A	HOH528
A	HOH531

site_id	AC4
Number of Residues	3
Details	binding site for residue SM A 404

Chain	Residue
A	GLU172
A	GLY209
A	GLU214

site_id	AC5
Number of Residues	4
Details	binding site for residue SM A 405

Chain	Residue
A	GLU207
A	HOH509
A	HOH523
A	HOH532

site_id	AC6
Number of Residues	6
Details	binding site for residue CA B 401

Chain	Residue
B	GLU116
B	ASN118
B	GLY121
B	ASP127
B	HOH508
B	HOH518

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

Chain	Residue
B	HIS115
B	GLY126
B	ASP162
B	ASP311
B	HOH509
B	HOH520

site_id	AC8
Number of Residues	6
Details	binding site for residue SM B 403

Chain	Residue
B	ASN289
B	GLU291
B	GLU303
B	HOH502
B	HOH503
B	HOH519

site_id	AC9
Number of Residues	3
Details	binding site for residue SM B 404

Chain	Residue
B	GLU172
B	GLY209
B	GLU214

site_id	AD1
Number of Residues	3
Details	binding site for residue SM B 405

Chain	Residue
B	GLU207
B	HOH507
B	HOH513

site_id	AD2
Number of Residues	1
Details	binding site for residue SM B 406

Chain	Residue
B	GLU90

site_id	AD3
Number of Residues	1
Details	binding site for residue SM B 407

Chain	Residue
B	GLU90

site_id	AD4
Number of Residues	6
Details	binding site for residue CA C 401

Chain	Residue
C	GLU116
C	ASN118
C	GLY121
C	ASP127
C	HOH502
C	HOH507

site_id	AD5
Number of Residues	6
Details	binding site for residue CA C 402

Chain	Residue
C	HIS115
C	GLY126
C	ASP162
C	ASP311
C	HOH503
C	HOH525

site_id	AD6
Number of Residues	7
Details	binding site for residue SM C 403

Chain	Residue
C	ASN289
C	GLU291
C	GLU303
C	HOH508
C	HOH516
C	HOH526
C	HOH529

site_id	AD7
Number of Residues	3
Details	binding site for residue SM C 404

Chain	Residue
C	GLU172
C	GLY209
C	GLU214

site_id	AD8
Number of Residues	2
Details	binding site for residue SM C 405

Chain	Residue
C	GLU207
C	HOH528

site_id	AD9
Number of Residues	2
Details	binding site for residue SM C 407

Chain	Residue
C	GLU90
C	ASP91

site_id	AE1
Number of Residues	6
Details	binding site for residue CA D 401

Chain	Residue
D	GLU116
D	ASN118
D	GLY121
D	ASP127
D	HOH507
D	HOH517

site_id	AE2
Number of Residues	6
Details	binding site for residue CA D 402

Chain	Residue
D	HIS115
D	GLY126
D	ASP162
D	ASP311
D	HOH504
D	HOH511

site_id	AE3
Number of Residues	7
Details	binding site for residue SM D 403

Chain	Residue
D	ASN289
D	GLU291
D	GLU303
D	HOH501
D	HOH503
D	HOH524
D	HOH525

site_id	AE4
Number of Residues	3
Details	binding site for residue SM D 404

Chain	Residue
D	GLU214
D	GLU172
D	GLY209

site_id	AE5
Number of Residues	2
Details	binding site for residue SM D 406

Chain	Residue
D	GLU90
D	ASP91

site_id	AE6
Number of Residues	6
Details	binding site for residue CA E 401

Chain	Residue
E	GLU116
E	ASN118
E	GLY121
E	ASP127
E	HOH516
E	HOH517

site_id	AE7
Number of Residues	6
Details	binding site for residue CA E 402

Chain	Residue
E	HIS115
E	GLY126
E	ASP162
E	ASP311
E	HOH519
E	HOH520

site_id	AE8
Number of Residues	7
Details	binding site for residue SM E 403

Chain	Residue
E	ASN289
E	GLU291
E	GLU303
E	HOH501
E	HOH503
E	HOH510
E	HOH525

site_id	AE9
Number of Residues	3
Details	binding site for residue SM E 404

Chain	Residue
E	GLU172
E	GLY209
E	GLU214

site_id	AF1
Number of Residues	1
Details	binding site for residue SM E 405

Chain	Residue
E	GLU90

site_id	AF2
Number of Residues	2
Details	binding site for residue SM E 406

Chain	Residue
E	GLU90
E	ASP91

site_id	AF3
Number of Residues	6
Details	binding site for residue CA F 401

Chain	Residue
F	GLU116
F	ASN118
F	GLY121
F	ASP127
F	HOH507
F	HOH518

site_id	AF4
Number of Residues	6
Details	binding site for residue CA F 402

Chain	Residue
F	HIS115
F	GLY126
F	ASP162
F	ASP311
F	HOH501
F	HOH520

site_id	AF5
Number of Residues	7
Details	binding site for residue SM F 403

Chain	Residue
F	ASN289
F	GLU291
F	GLU303
F	HOH502
F	HOH519
F	HOH526
F	HOH527

site_id	AF6
Number of Residues	3
Details	binding site for residue SM F 404

Chain	Residue
F	GLU172
F	GLY209
F	GLU214

site_id	AF7
Number of Residues	1
Details	binding site for residue SM F 406

Chain	Residue
F	GLU90

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	66
Details	BINDING: BINDING => ECO:0000269\|PubMed:26755729, ECO:0007744\|PDB:4WMO, ECO:0007744\|PDB:4WN0

Chain	Residue	Details
A	HIS115
A	GLU303
A	ASP311
B	HIS115
B	GLU116
B	ASN118
B	GLY121
B	GLY126
B	ASP127
B	ASP162
B	ASN289
A	GLU116
B	GLU291
B	GLU303
B	ASP311
C	HIS115
C	GLU116
C	ASN118
C	GLY121
C	GLY126
C	ASP127
C	ASP162
A	ASN118
C	ASN289
C	GLU291
C	GLU303
C	ASP311
D	HIS115
D	GLU116
D	ASN118
D	GLY121
D	GLY126
D	ASP127
A	GLY121
D	ASP162
D	ASN289
D	GLU291
D	GLU303
D	ASP311
E	HIS115
E	GLU116
E	ASN118
E	GLY121
E	GLY126
A	GLY126
E	ASP127
E	ASP162
E	ASN289
E	GLU291
E	GLU303
E	ASP311
F	HIS115
F	GLU116
F	ASN118
F	GLY121
A	ASP127
F	GLY126
F	ASP127
F	ASP162
F	ASN289
F	GLU291
F	GLU303
F	ASP311
A	ASP162
A	ASN289
A	GLU291

site_id	SWS_FT_FI2
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305\|PubMed:15537792

Chain	Residue	Details
A	ASN192
B	ASN192
C	ASN192
D	ASN192
E	ASN192
F	ASN192

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