4PCR

Crystal structure of Canavalia brasiliensis seed lectin (ConBr) complexed with Gamma-Aminobutyric Acid (GABA)

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	0046872	molecular_function	metal ion binding
A	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	0046872	molecular_function	metal ion binding
D	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CA A 301

Chain	Residue
A	ASP10
A	TYR12
A	ASN14
A	ASP19
A	HOH444
A	HOH446

---

site_id	AC2
Number of Residues	6
Details	binding site for residue MN A 302

Chain	Residue
A	HIS24
A	HOH422
A	HOH441
A	GLU8
A	ASP10
A	ASP19

---

site_id	AC3
Number of Residues	7
Details	binding site for residue IPA A 303

Chain	Residue
A	TYR12
A	ASN14
A	GLY98
A	LEU99
A	TYR100
A	ALA207
A	ASP208

---

site_id	AC4
Number of Residues	9
Details	binding site for residue ABU A 304

Chain	Residue
A	SER113
A	LEU115
A	ASN124
A	ALA125
A	LEU126
A	VAL179
A	HIS180
A	HOH418
D	ASP139

---

site_id	AC5
Number of Residues	3
Details	binding site for residue ABU A 305

Chain	Residue
A	ASN124
A	GLU183
D	GLN132

---

site_id	AC6
Number of Residues	2
Details	binding site for residue PEG A 306

Chain	Residue
A	THR49
A	HOH409

---

site_id	AC7
Number of Residues	6
Details	binding site for residue CA D 301

Chain	Residue
D	ASP10
D	TYR12
D	ASN14
D	ASP19
D	HOH447
D	HOH448

---

site_id	AC8
Number of Residues	6
Details	binding site for residue MN D 302

Chain	Residue
D	GLU8
D	ASP10
D	ASP19
D	HIS24
D	HOH423
D	HOH443

---

site_id	AC9
Number of Residues	7
Details	binding site for residue IPA D 303

Chain	Residue
D	TYR12
D	ASN14
D	GLY98
D	LEU99
D	TYR100
D	ALA207
D	ASP208

---

site_id	AD1
Number of Residues	5
Details	binding site for residue ABU D 304

Chain	Residue
A	TYR100
A	GLN132
A	PHE133
D	ASN124
D	GLU183

---

site_id	AD2
Number of Residues	3
Details	binding site for residue EDO D 305

Chain	Residue
D	GLY18
D	SER161
D	EDO306

---

site_id	AD3
Number of Residues	3
Details	binding site for residue EDO D 306

Chain	Residue
D	LYS36
D	THR37
D	EDO305

---

site_id	AD4
Number of Residues	3
Details	binding site for residue PEG D 307

Chain	Residue
D	LYS46
D	VAL47
D	PRO68

---

site_id	AD5
Number of Residues	5
Details	binding site for residue PEG D 308

Chain	Residue
D	LEU107
D	ASN131
D	GLN132
D	GLY152
D	ASN153

---

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	14
Details	BINDING:

Chain	Residue	Details
A	GLU8
D	TYR12
D	ASN14
D	ASP19
D	HIS24
D	LEU99
A	ASP10
A	TYR12
A	ASN14
A	ASP19
A	HIS24
A	LEU99
D	GLU8
D	ASP10

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	SER34
A	ASP208
D	SER34
D	ASP208

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:10506175

Chain	Residue	Details
A	ARG228
D	ARG228

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