1JDY

RABBIT MUSCLE PHOSPHOGLUCOMUTASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004614	molecular_function	phosphoglucomutase activity
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	0016529	cellular_component	sarcoplasmic reticulum
A	0016853	molecular_function	isomerase activity
A	0016868	molecular_function	intramolecular phosphotransferase activity
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0004614	molecular_function	phosphoglucomutase activity
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	0016529	cellular_component	sarcoplasmic reticulum
B	0016853	molecular_function	isomerase activity
B	0016868	molecular_function	intramolecular phosphotransferase activity
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 562

Chain	Residue
A	ASP287
A	ASP289
A	ASP291
A	SEP116

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 563

Chain	Residue
A	THR356
A	ARG502

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B 562

Chain	Residue
B	SEP116
B	ASP287
B	ASP289
B	ASP291

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 563

Chain	Residue
B	ARG502
B	SER504
B	ARG514

---

site_id	MBA
Number of Residues	4
Details	METAL ATOM IN 562, ASP RESIDUES 287, 289, 291.

Chain	Residue
A	ASP287
A	ASP289
A	ASP291
A	SEP116

---

site_id	MBB
Number of Residues	4
Details	METAL ATOM IN 562, ASP RESIDUES 287, 289, 291.

Chain	Residue
B	ASP287
B	ASP289
B	ASP291
B	SEP116

---

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	GLY110-PRO119

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Phosphoserine intermediate => ECO:0000269|PubMed:5669853

Chain	Residue	Details
A	HIS117
B	HIS117

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1C47

Chain	Residue	Details
A	LYS23
B	GLU376
B	PHE378
B	ASP389
A	ASN293
A	GLY357
A	GLU376
A	PHE378
A	ASP389
B	LYS23
B	ASN293
B	GLY357

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: via phosphate group => ECO:0000269|PubMed:15299905, ECO:0007744|PDB:3PMG

Chain	Residue	Details
A	HIS117
B	HIS117

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:15299905, ECO:0007744|PDB:3PMG

Chain	Residue	Details
A	GLY288
A	GLY290
A	ARG292
B	GLY288
B	GLY290
B	ARG292

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P36871

Chain	Residue	Details
A	VAL1
B	VAL1

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P36871

Chain	Residue	Details
A	PRO16
B	PRO16

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9D0F9

Chain	Residue	Details
A	ALA115
A	GLY507
B	ALA115
B	GLY507

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15299905, ECO:0007744|PDB:3PMG

Chain	Residue	Details
A	HIS117
B	HIS117

---

site_id	SWS_FT_FI9
Number of Residues	10
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P38652

Chain	Residue	Details
A	ASN134
B	ILE541
A	GLY213
A	LYS369
A	LYS485
A	ILE541
B	ASN134
B	GLY213
B	LYS369
B	LYS485

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P36871

Chain	Residue	Details
A	VAL185
B	VAL185

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9D0F9

Chain	Residue	Details
A	ILE349
B	ILE349

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9D0F9

Chain	Residue	Details
A	GLU353
B	GLU353

---

site_id	SWS_FT_FI13
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P36871

Chain	Residue	Details
A	PHE378
A	GLY505
A	ALA509
B	PHE378
B	GLY505
B	ALA509

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9D0F9

Chain	Residue	Details
A	PHE419
B	PHE419

---

site_id	SWS_FT_FI15
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PAK1 => ECO:0000250|UniProtKB:P36871

Chain	Residue	Details
A	VAL467
B	VAL467

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 352

Chain	Residue	Details
A	HIS117	activator, covalently attached, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor
A	ASN118	proton acceptor, proton donor
A	GLY288	metal ligand
A	GLY290	metal ligand
A	ARG292	metal ligand
A	ASN293	electrostatic stabiliser
A	ASP389	proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	7
Details	M-CSA 352

Chain	Residue	Details
B	HIS117	activator, covalently attached, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor
B	ASN118	proton acceptor, proton donor
B	GLY288	metal ligand
B	GLY290	metal ligand
B	ARG292	metal ligand
B	ASN293	electrostatic stabiliser
B	ASP389	proton acceptor, proton donor

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