4FNS

Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004557	molecular_function	alpha-galactosidase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0033531	biological_process	stachyose metabolic process
A	0034484	biological_process	raffinose catabolic process
A	0051289	biological_process	protein homotetramerization
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0004557	molecular_function	alpha-galactosidase activity
B	0005975	biological_process	carbohydrate metabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0033531	biological_process	stachyose metabolic process
B	0034484	biological_process	raffinose catabolic process
B	0051289	biological_process	protein homotetramerization
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0004557	molecular_function	alpha-galactosidase activity
C	0005975	biological_process	carbohydrate metabolic process
C	0016052	biological_process	carbohydrate catabolic process
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0033531	biological_process	stachyose metabolic process
C	0034484	biological_process	raffinose catabolic process
C	0051289	biological_process	protein homotetramerization
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0004557	molecular_function	alpha-galactosidase activity
D	0005975	biological_process	carbohydrate metabolic process
D	0016052	biological_process	carbohydrate catabolic process
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0033531	biological_process	stachyose metabolic process
D	0034484	biological_process	raffinose catabolic process
D	0051289	biological_process	protein homotetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DGJ A 801

Chain	Residue
A	TRP336
A	GLY528
A	GLY529
A	TRP545
A	ASP548
A	HOH999
A	ASP366
A	ASP367
A	TRP411
A	ARG443
A	LYS476
A	ASP478
A	ASN480
A	CYS526

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 802

Chain	Residue
A	GLY200
A	ARG201
A	TRP204
A	ASN549
A	SER554
C	ALA670
C	GLU671
C	ALA672

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 803

Chain	Residue
A	ASP139
A	ALA140
A	GLY143
A	LEU144

---

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DGJ B 801

Chain	Residue
B	TRP336
B	ASP366
B	ASP367
B	TRP411
B	ARG443
B	LYS476
B	ASP478
B	ASN480
B	CYS526
B	GLY528
B	GLY529
B	TRP545
B	ASP548
B	HOH1078

---

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 B 802

Chain	Residue
B	GLY200
B	ARG201
B	TRP204
B	ASN549
B	SER554
B	VAL583
B	HOH977
D	ALA670
D	GLU671
D	ALA672
D	HOH1079

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 803

Chain	Residue
B	LYS105
B	GLY138
B	ASP139
B	ALA140
B	GLY143
B	LEU144
B	GLU145

---

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DGJ C 801

Chain	Residue
C	TRP336
C	ASP366
C	ASP367
C	TRP411
C	ARG443
C	LYS476
C	ASP478
C	ASN480
C	CYS526
C	GLY528
C	GLY529
C	TRP545
C	ASP548
C	HOH1037

---

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 C 802

Chain	Residue
A	ALA670
A	GLU671
A	ALA672
C	GLY200
C	ARG201
C	TRP204
C	ASN549
C	SER554
C	HOH962

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 803

Chain	Residue
C	LYS105
C	GLY138
C	ASP139
C	GLY143
C	LEU144

---

site_id	BC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DGJ D 801

Chain	Residue
D	TRP336
D	ASP366
D	ASP367
D	TRP411
D	ARG443
D	LYS476
D	ASP478
D	ASN480
D	CYS526
D	GLY528
D	GLY529
D	TRP545
D	ASP548

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 802

Chain	Residue
D	LEU176
D	PRO277
D	PHE280
D	THR281

---

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 D 803

Chain	Residue
B	GLU671
B	ALA672
D	GLY200
D	ARG201
D	TRP204
D	ASN549
D	SER554
D	VAL583
D	HOH1133

---

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 804

Chain	Residue
A	GLY694
D	LYS105
D	ASP139
D	GLY143
D	LEU144
D	GLU145
D	LYS168

---

Functional Information from PROSITE/UniProt

site_id	PS00512
Number of Residues	16
Details	ALPHA_GALACTOSIDASE Alpha-galactosidase signature. GIelVvLDDg.Wfge....RD

Chain	Residue	Details
A	GLY359-ASP374

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:23012371

Chain	Residue	Details
A	ASP478
B	ASP478
C	ASP478
D	ASP478

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:23012371

Chain	Residue	Details
A	ASP548
B	ASP548
C	ASP548
D	ASP548

---

site_id	SWS_FT_FI3
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269|PubMed:23012371, ECO:0007744|PDB:4FNT

Chain	Residue	Details
C	ASP548
D	ASP53
D	TRP199
D	ASP366
D	ARG443
D	LYS476
D	CYS526
D	ASP548
A	ASP53
A	TRP199
A	ASP366
A	ARG443
A	LYS476
A	CYS526
A	ASP548
B	ASP53
B	TRP199
B	ASP366
B	ARG443
B	LYS476
B	CYS526
B	ASP548
C	ASP53
C	TRP199
C	ASP366
C	ARG443
C	LYS476
C	CYS526

---