3UJE

Asymmetric complex of human neuron specific enolase-3-PGA/PEP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000015	cellular_component	phosphopyruvate hydratase complex
A	0000287	molecular_function	magnesium ion binding
A	0001917	cellular_component	photoreceptor inner segment
A	0004634	molecular_function	phosphopyruvate hydratase activity
A	0005515	molecular_function	protein binding
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016020	cellular_component	membrane
A	0016829	molecular_function	lyase activity
A	0043025	cellular_component	neuronal cell body
A	0043204	cellular_component	perikaryon
A	0046872	molecular_function	metal ion binding
A	0061621	biological_process	canonical glycolysis
A	0070062	cellular_component	extracellular exosome
B	0000015	cellular_component	phosphopyruvate hydratase complex
B	0000287	molecular_function	magnesium ion binding
B	0001917	cellular_component	photoreceptor inner segment
B	0004634	molecular_function	phosphopyruvate hydratase activity
B	0005515	molecular_function	protein binding
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016020	cellular_component	membrane
B	0016829	molecular_function	lyase activity
B	0043025	cellular_component	neuronal cell body
B	0043204	cellular_component	perikaryon
B	0046872	molecular_function	metal ion binding
B	0061621	biological_process	canonical glycolysis
B	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 501

Chain	Residue
A	ASP244
A	GLU292
A	ASP317
A	2PG503
A	HOH679

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 502

Chain	Residue
A	SER39
A	2PG503
A	HOH680
A	HOH681

---

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 2PG A 503

Chain	Residue
A	GLY37
A	ALA38
A	SER39
A	HIS157
A	GLN165
A	GLU166
A	GLU209
A	ASP244
A	GLU292
A	ASP317
A	LEU340
A	LYS342
A	HIS370
A	ARG371
A	SER372
A	LYS393
A	MG501
A	MG502
A	HOH680
A	HOH681

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRS A 504

Chain	Residue
A	THR40
A	ILE42
A	SER248
A	GLU249
A	GLN297
A	HOH748
A	HOH786
A	HOH827

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 501

Chain	Residue
B	ASP244
B	GLU292
B	ASP317
B	PEP503
B	HOH679

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 502

Chain	Residue
B	SER39
B	PEP503
B	HOH680
B	HOH681

---

site_id	AC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PEP B 503

Chain	Residue
B	GLY37
B	ALA38
B	SER39
B	GLN165
B	GLU209
B	ASP244
B	GLU292
B	ASP317
B	LYS342
B	HIS370
B	ARG371
B	SER372
B	LYS393
B	MG501
B	MG502
B	HOH680
B	HOH681

---

Functional Information from PROSITE/UniProt

site_id	PS00164
Number of Residues	14
Details	ENOLASE Enolase signature. LLLKvNQIGSVTEA

Chain	Residue	Details
A	LEU339-ALA352

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P00924

Chain	Residue	Details
A	GLU209
B	GLU209

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00924

Chain	Residue	Details
A	LYS342
B	LYS342

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P06733

Chain	Residue	Details
A	SER39
B	SER39

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P00924

Chain	Residue	Details
A	HIS157
B	ASP317
B	SER369
B	LYS393
A	GLU166
A	GLU292
A	ASP317
A	SER369
A	LYS393
B	HIS157
B	GLU166
B	GLU292

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	ASP244
B	ASP244

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P06733

Chain	Residue	Details
A	SER1
B	SER1

---

site_id	SWS_FT_FI7
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06733

Chain	Residue	Details
A	LYS4
A	LYS63
A	LYS192
A	LYS255
B	LYS4
B	LYS63
B	LYS192
B	LYS255

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231

Chain	Residue	Details
A	THR25
B	THR25

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455

Chain	Residue	Details
A	TYR43
B	TYR43

---

site_id	SWS_FT_FI10
Number of Residues	6
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182

Chain	Residue	Details
A	LYS59
A	LYS88
A	LYS227
B	LYS59
B	LYS88
B	LYS227

---

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17183

Chain	Residue	Details
A	LYS196
A	LYS198
B	LYS196
B	LYS198

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182

Chain	Residue	Details
A	LYS201
B	LYS201

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733

Chain	Residue	Details
A	LYS232
B	LYS232

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER262
B	SER262

---

site_id	SWS_FT_FI15
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06733

Chain	Residue	Details
A	TYR286
B	TYR286

---

site_id	SWS_FT_FI16
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06733

Chain	Residue	Details
A	SER290
B	SER290

---

site_id	SWS_FT_FI17
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17182

Chain	Residue	Details
A	LYS334
A	LYS342
A	LYS405
B	LYS334
B	LYS342
B	LYS405

---

site_id	SWS_FT_FI18
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P06733

Chain	Residue	Details
A	LYS201
B	LYS201

---