7KB6

Co-crystal structure of alpha glucosidase with compound 7

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
A	0030246	molecular_function	carbohydrate binding
B	0001701	biological_process	in utero embryonic development
B	0001889	biological_process	liver development
B	0003723	molecular_function	RNA binding
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005783	cellular_component	endoplasmic reticulum
B	0006491	biological_process	N-glycan processing
B	0010977	biological_process	negative regulation of neuron projection development
B	0017177	cellular_component	glucosidase II complex
B	0043231	cellular_component	intracellular membrane-bounded organelle
B	0044877	molecular_function	protein-containing complex binding
B	0046872	molecular_function	metal ion binding
B	0071941	biological_process	nitrogen cycle metabolic process
C	0003824	molecular_function	catalytic activity
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005975	biological_process	carbohydrate metabolic process
C	0030246	molecular_function	carbohydrate binding
D	0001701	biological_process	in utero embryonic development
D	0001889	biological_process	liver development
D	0003723	molecular_function	RNA binding
D	0005509	molecular_function	calcium ion binding
D	0005515	molecular_function	protein binding
D	0005783	cellular_component	endoplasmic reticulum
D	0006491	biological_process	N-glycan processing
D	0010977	biological_process	negative regulation of neuron projection development
D	0017177	cellular_component	glucosidase II complex
D	0043231	cellular_component	intracellular membrane-bounded organelle
D	0044877	molecular_function	protein-containing complex binding
D	0046872	molecular_function	metal ion binding
D	0071941	biological_process	nitrogen cycle metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DDNMDGMVSlaEL

Chain	Residue	Details
B	ASP222-LEU234

---

site_id	PS00129
Number of Residues	8
Details	GLYCOSYL_HYDROL_F31_1 Glycosyl hydrolases family 31 active site. YVWnDMNE

Chain	Residue	Details
A	TYR560-GLU567

---

site_id	PS00707
Number of Residues	31
Details	GLYCOSYL_HYDROL_F31_2 Glycosyl hydrolases family 31 signature 2. GADVGGFfknPepeLLvRWyqMGAYqPFfRA

Chain	Residue	Details
A	GLY667-ALA697

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27462106","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5HJR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"27462106","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27462106","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5HJO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q14697","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10921916","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27462106","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5F0E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5HJO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5HJR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IED","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IEF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IEG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	68
Details	Domain: {"description":"LDL-receptor class A 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	88
Details	Domain: {"description":"LDL-receptor class A 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27462106","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5HJO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27462106","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5F0E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5H9O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5HJO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5HJR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IED","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IEF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IEG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---