5M1I

Structure of GH36 alpha-galactosidase from Thermotoga maritima in a covalent complex with a cyclopropyl carbasugar.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004557	molecular_function	alpha-galactosidase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0016139	biological_process	glycoside catabolic process
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0030246	molecular_function	carbohydrate binding
A	0042803	molecular_function	protein homodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue SO4 A 601

Chain	Residue
A	HIS-3
A	HOH917
A	SER-4
A	MET-2
A	GLY-5
A	LYS111
A	ASN290
A	TRP291
A	ASN292
A	HOH806

---

site_id	AC2
Number of Residues	4
Details	binding site for residue SO4 A 602

Chain	Residue
A	LYS302
A	ASP303
A	GLU304
A	LYS339

---

site_id	AC3
Number of Residues	6
Details	binding site for residue SO4 A 603

Chain	Residue
A	ARG9
A	TRP392
A	GLY393
A	GLU394
A	HOH760
A	HOH847

---

site_id	AC4
Number of Residues	3
Details	binding site for residue SO4 A 604

Chain	Residue
A	GLU434
A	LYS435
A	THR436

---

site_id	AC5
Number of Residues	5
Details	binding site for residue SO4 A 605

Chain	Residue
A	ARG349
A	GLU353
A	HOH702
A	HOH722
A	HOH748

---

site_id	AC6
Number of Residues	4
Details	binding site for residue SO4 A 606

Chain	Residue
A	PHE143
A	ASP144
A	ASP145
A	HOH733

---

site_id	AC7
Number of Residues	13
Details	binding site for residue 7D8 A 607

Chain	Residue
A	SER-4
A	TRP65
A	TRP190
A	TYR191
A	ASP220
A	ASP221
A	TRP257
A	LYS325
A	ASP327
A	PHE328
A	CYS368
A	ARG383
A	ASP387

---

site_id	AC8
Number of Residues	5
Details	binding site for residue EDO A 608

Chain	Residue
A	ARG-6
A	ASP387
A	GLY400
A	PRO402
A	EDO609

---

site_id	AC9
Number of Residues	6
Details	binding site for residue EDO A 609

Chain	Residue
A	ARG-6
A	TRP65
A	THR88
A	GLY400
A	EDO608
A	EDO612

---

site_id	AD1
Number of Residues	6
Details	binding site for residue EDO A 610

Chain	Residue
A	ALA-1
A	PRO402
A	HOH761
A	HOH772
A	HOH802
A	HOH822

---

site_id	AD2
Number of Residues	2
Details	binding site for residue EDO A 611

Chain	Residue
A	LYS181
A	HIS182

---

site_id	AD3
Number of Residues	8
Details	binding site for residue EDO A 612

Chain	Residue
A	GLN63
A	TRP65
A	GLY66
A	THR88
A	ASN399
A	EDO609
A	EDO616
A	HOH898

---

site_id	AD4
Number of Residues	6
Details	binding site for residue EDO A 613

Chain	Residue
A	LYS357
A	ARG496
A	VAL512
A	ASP514
A	GLU519
A	HOH701

---

site_id	AD5
Number of Residues	6
Details	binding site for residue EDO A 614

Chain	Residue
A	SER-12
A	HIS-13
A	ARG405
A	HOH764
A	HOH843
A	HOH870

---

site_id	AD6
Number of Residues	6
Details	binding site for residue EDO A 615

Chain	Residue
A	LYS28
A	ILE29
A	HIS30
A	LEU31
A	HOH804
A	HOH819

---

site_id	AD7
Number of Residues	7
Details	binding site for residue EDO A 616

Chain	Residue
A	ARG-6
A	ILE81
A	ASP82
A	THR88
A	EDO612
A	HOH876
A	HOH936

---

site_id	AD8
Number of Residues	3
Details	binding site for residue EDO A 617

Chain	Residue
A	ASP362
A	PRO184
A	ARG322

---

site_id	AD9
Number of Residues	1
Details	binding site for residue EDO A 618

Chain	Residue
A	GLY235

---

site_id	AE1
Number of Residues	5
Details	binding site for residue EDO A 619

Chain	Residue
A	ARG45
A	ASN99
A	GLU128
A	TYR135
A	HOH785

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:17323919

Chain	Residue	Details
A	ASP327

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:17323919

Chain	Residue	Details
A	ASP387

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:27783466, ECO:0007744|PDB:5M16

Chain	Residue	Details
A	TRP65
A	TYR191
A	ASP220
A	LYS325
A	CYS368
A	ARG383

---