2Q4H

Ensemble refinement of the crystal structure of GALT-like protein from Arabidopsis thaliana At5g18200

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005975	biological_process	carbohydrate metabolic process
A	0006006	biological_process	glucose metabolic process
A	0006012	biological_process	galactose metabolic process
A	0008108	molecular_function	UDP-glucose:hexose-1-phosphate uridylyltransferase activity
A	0008270	molecular_function	zinc ion binding
A	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0017103	molecular_function	UTP:galactose-1-phosphate uridylyltransferase activity
A	0043531	molecular_function	ADP binding
A	0046872	molecular_function	metal ion binding
A	0047345	molecular_function	ribose-5-phosphate adenylyltransferase activity
A	0080040	biological_process	positive regulation of cellular response to phosphate starvation
B	0005975	biological_process	carbohydrate metabolic process
B	0006006	biological_process	glucose metabolic process
B	0006012	biological_process	galactose metabolic process
B	0008108	molecular_function	UDP-glucose:hexose-1-phosphate uridylyltransferase activity
B	0008270	molecular_function	zinc ion binding
B	0016740	molecular_function	transferase activity
B	0016779	molecular_function	nucleotidyltransferase activity
B	0017103	molecular_function	UTP:galactose-1-phosphate uridylyltransferase activity
B	0043531	molecular_function	ADP binding
B	0046872	molecular_function	metal ion binding
B	0047345	molecular_function	ribose-5-phosphate adenylyltransferase activity
B	0080040	biological_process	positive regulation of cellular response to phosphate starvation

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 603

Chain	Residue
A	CYS63
A	CYS66
A	HIS133
A	HIS184

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 604

Chain	Residue
A	CYS216
A	CYS219
A	HIS255
A	HIS310

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 605

Chain	Residue
B	PHE65
B	CYS66
B	HIS133
B	HIS184
B	CYS63

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 606

Chain	Residue
B	CYS216
B	CYS219
B	HIS255

---

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE AMP A 601

Chain	Residue
A	GLU72
A	CYS73
A	ALA74
A	ILE92
A	GLU93
A	ASN94
A	LEU95
A	TYR96
A	ASN173
A	GLY179
A	ALA180
A	SER181
A	MET182
A	HIS186
A	GLN188
A	HOH611
A	HOH768
A	HOH769
A	HOH770

---

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EDO A 607

Chain	Residue
A	PRO239
A	ALA242
A	TYR244
A	PRO245
A	PHE246
A	GLU247
A	ASN334
A	VAL336
A	PRO338
A	VAL341

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 608

Chain	Residue
A	THR31
A	THR198
A	GLN314
A	HOH616
A	HOH635
A	HOH668
A	HOH776

---

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 609

Chain	Residue
A	TYR244
A	VAL316
A	GLN318
A	SER320
A	HOH632
A	HOH661
A	HOH744

---

site_id	AC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AMP B 602

Chain	Residue
B	PHE65
B	GLU72
B	CYS73
B	ALA74
B	ILE92
B	GLU93
B	ASN94
B	LEU95
B	ALA180
B	SER181
B	MET182
B	HIS186
B	GLN188
B	HOH680
B	HOH735

---

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO B 610

Chain	Residue
B	ALA242
B	TYR244
B	PRO245
B	PHE246
B	GLU247
B	ASN334
B	VAL336
B	PRO338
B	VAL341

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 611

Chain	Residue
B	HIS295
B	GLN314
B	HOH636
B	HOH679
B	HOH695
B	HOH819

---

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 612

Chain	Residue
A	ILE327
B	TYR244
B	VAL316
B	GLN318
B	SER320
B	HOH647
B	HOH688
B	HOH704

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Tele-AMP-histidine intermediate","evidences":[{"source":"PubMed","id":"16519510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17850744","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16519510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17850744","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of an ADP-glucose phosphorylase from Arabidopsis thaliana with bound ADP-glucose.","authors":["McCoy J.G.","Wesenberg G.E.","Phillips G.N. Jr.","Bitto E.","Bingman C.A."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of an ADP-glucose phosphorylase from Arabidopsis thaliana with bound ADP-glucose.","authors":["McCoy J.G.","Wesenberg G.E.","Phillips G.N. Jr.","Bitto E.","Bingman C.A."]}}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1hxq

Chain	Residue	Details
A	HIS186
A	ALA180
A	HIS184
A	GLN188

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1hxq

Chain	Residue	Details
B	HIS186
B	ALA180
B	HIS184
B	GLN188

---