5VEC

Crystal Structure of the R515L missense variant of human PGM1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004614	molecular_function	phosphoglucomutase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0006006	biological_process	glucose metabolic process
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016853	molecular_function	isomerase activity
A	0016868	molecular_function	intramolecular phosphotransferase activity
A	0033499	biological_process	galactose catabolic process via UDP-galactose, Leloir pathway
A	0046872	molecular_function	metal ion binding
A	0070062	cellular_component	extracellular exosome
A	1904724	cellular_component	tertiary granule lumen
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0000287	molecular_function	magnesium ion binding
B	0004614	molecular_function	phosphoglucomutase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0006006	biological_process	glucose metabolic process
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016853	molecular_function	isomerase activity
B	0016868	molecular_function	intramolecular phosphotransferase activity
B	0033499	biological_process	galactose catabolic process via UDP-galactose, Leloir pathway
B	0046872	molecular_function	metal ion binding
B	0070062	cellular_component	extracellular exosome
B	1904724	cellular_component	tertiary granule lumen
B	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue SO4 A 601

Chain	Residue
A	ARG503
A	SER505
A	GLY506

---

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

Chain	Residue
A	ASN179
A	LYS470
A	ARG491
A	HOH862

---

site_id	AC3
Number of Residues	5
Details	binding site for residue SO4 A 603

Chain	Residue
A	PRO244
A	ASN246
A	HOH724
A	ARG217
A	ARG221

---

site_id	AC4
Number of Residues	2
Details	binding site for residue SO4 A 604

Chain	Residue
A	ARG23
A	HOH704

---

site_id	AC5
Number of Residues	6
Details	binding site for residue MG A 605

Chain	Residue
A	SER117
A	ASP288
A	ASP290
A	ASP292
A	HOH726
A	HOH766

---

site_id	AC6
Number of Residues	3
Details	binding site for residue GOL A 606

Chain	Residue
A	PRO244
A	ALA245
A	HOH714

---

site_id	AC7
Number of Residues	8
Details	binding site for residue GOL A 607

Chain	Residue
A	PHE65
A	TYR66
A	MET67
A	LYS68
A	GLU69
A	GLU255
A	HOH723
A	HOH819

---

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

Chain	Residue
A	GLU432
A	VAL433
A	GLU434
A	THR553
A	ARG555

---

site_id	AC9
Number of Residues	3
Details	binding site for residue SO4 B 601

Chain	Residue
B	ARG503
B	SER505
B	GLY506

---

site_id	AD1
Number of Residues	3
Details	binding site for residue SO4 B 602

Chain	Residue
B	ARG293
B	ARG427
B	HOH809

---

site_id	AD2
Number of Residues	6
Details	binding site for residue MG B 603

Chain	Residue
B	SER117
B	ASP288
B	ASP290
B	ASP292
B	HOH720
B	HOH742

---

site_id	AD3
Number of Residues	6
Details	binding site for residue GOL B 604

Chain	Residue
B	THR19
B	SER20
B	GLY358
B	TRP359
B	GLU376
B	GOL605

---

site_id	AD4
Number of Residues	8
Details	binding site for residue GOL B 605

Chain	Residue
B	THR19
B	LYS130
B	PRO138
B	ASP292
B	TRP359
B	LYS389
B	GOL604
B	HOH870

---

site_id	AD5
Number of Residues	4
Details	binding site for residue GOL B 606

Chain	Residue
B	GLN41
B	SER45
B	ARG52
B	ASN81

---

Functional Information from PROSITE/UniProt

site_id	PS00710
Number of Residues	10
Details	PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GIiLTASHNP

Chain	Residue	Details
A	GLY111-PRO120

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Phosphoserine intermediate","evidences":[{"source":"PubMed","id":"25288802","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00949","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"description":"via phosphate groupe","evidences":[{"source":"PubMed","id":"25288802","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26972339","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EPC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F9C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"25288802","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P38652","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	10
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by PAK1","evidences":[{"source":"PubMed","id":"15378030","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---