1TE6

Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom

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	6
Details	BINDING SITE FOR RESIDUE MG A 640

Chain	Residue
A	ASP244
A	GLU292
A	ASP317
A	HOH744
A	HOH745
A	HOH746

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 641

Chain	Residue
A	HOH747
A	HOH748
A	SER39
A	PO4642
A	HOH744

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 A 642

Chain	Residue
A	GLY37
A	ALA38
A	SER39
A	HIS157
A	LYS342
A	ARG371
A	SER372
A	MG641
A	HOH744
A	HOH748
A	HOH811

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 740

Chain	Residue
B	ASP244
B	GLU292
B	ASP317
B	HOH749
B	HOH750
B	HOH751

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 742

Chain	Residue
B	LYS342
B	ARG371
B	SER372

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS A 660

Chain	Residue
A	THR40
A	GLU249
A	GLN297
A	HOH869
A	HOH892
A	HOH894
A	HOH927

---

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	GLY210
B	GLY210

---

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

Chain	Residue	Details
A	VAL343
B	VAL343

---

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

Chain	Residue	Details
A	THR40
B	THR40

---

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

Chain	Residue	Details
A	ALA158
B	ASP318
B	HIS370
B	THR394
A	PHE167
A	ASP293
A	ASP318
A	HIS370
A	THR394
B	ALA158
B	PHE167
B	ASP293

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	VAL245
B	VAL245

---

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

Chain	Residue	Details
A	ILE2
B	ILE2

---

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

Chain	Residue	Details
A	ILE5
A	ALA64
A	GLY193
A	TYR256
B	ILE5
B	ALA64
B	GLY193
B	TYR256

---

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

Chain	Residue	Details
A	ALA26
B	ALA26

---

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

Chain	Residue	Details
A	GLU44
B	GLU44

---

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

Chain	Residue	Details
A	GLY60
A	LEU89
A	GLU228
B	GLY60
B	LEU89
B	GLU228

---

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

Chain	Residue	Details
A	ASP197
A	TYR199
B	ASP197
B	TYR199

---

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

Chain	Residue	Details
A	ASP202
B	ASP202

---

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

Chain	Residue	Details
A	ALA233
B	ALA233

---

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

Chain	Residue	Details
A	PRO263
B	PRO263

---

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

Chain	Residue	Details
A	PRO287
B	PRO287

---

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

Chain	Residue	Details
A	ILE291
B	ILE291

---

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

Chain	Residue	Details
A	ALA335
A	VAL343
A	TYR406
B	ALA335
B	VAL343
B	TYR406

---

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	ASP202
B	ASP202

---