5TIJ

Structure of Human Enolase 2 with ((3S,5S)-1,5-dihydroxy-3-methyl-2-oxopyrrolidin-3-yl)phosphonate (purified enantiomer)

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	15
Details	binding site for residue 5TX A 501

Chain	Residue
A	GLY38
A	LYS343
A	HIS371
A	ARG372
A	SER373
A	LYS394
A	MG502
A	ALA39
A	SER40
A	GLN166
A	GLU167
A	ASP245
A	GLU293
A	ASP318
A	LEU341

---

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 502

Chain	Residue
A	ASP245
A	GLU293
A	ASP318
A	5TX501
A	HOH622

---

site_id	AC3
Number of Residues	16
Details	binding site for residue 5TX B 501

Chain	Residue
B	GLY38
B	ALA39
B	SER40
B	GLN166
B	GLU167
B	GLU210
B	ASP245
B	GLU293
B	ASP318
B	LEU341
B	LYS343
B	HIS371
B	ARG372
B	SER373
B	LYS394
B	MG502

---

site_id	AC4
Number of Residues	5
Details	binding site for residue MG B 502

Chain	Residue
B	ASP245
B	GLU293
B	ASP318
B	5TX501
B	HOH609

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU340-ALA353

---

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	GLU210
B	GLU210

---

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

Chain	Residue	Details
A	LYS343
B	LYS343

---

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

Chain	Residue	Details
A	SER40
B	SER40

---

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

Chain	Residue	Details
A	HIS158
B	ASP318
B	SER370
B	LYS394
A	GLU167
A	GLU293
A	ASP318
A	SER370
A	LYS394
B	HIS158
B	GLU167
B	GLU293

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	ASP245
B	ASP245

---

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

Chain	Residue	Details
A	SER2
B	SER2

---

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

Chain	Residue	Details
A	LYS5
A	LYS64
A	LYS193
A	LYS256
B	LYS5
B	LYS64
B	LYS193
B	LYS256

---

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

Chain	Residue	Details
A	THR26
B	THR26

---

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

Chain	Residue	Details
A	TYR44
B	TYR44

---

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

Chain	Residue	Details
A	LYS60
A	LYS89
A	LYS228
B	LYS60
B	LYS89
B	LYS228

---

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

Chain	Residue	Details
A	LYS197
A	LYS199
B	LYS197
B	LYS199

---

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

Chain	Residue	Details
A	LYS202
B	LYS202

---

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

Chain	Residue	Details
A	LYS233
B	LYS233

---

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

Chain	Residue	Details
A	SER263
B	SER263

---

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

Chain	Residue	Details
A	TYR287
B	TYR287

---

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

Chain	Residue	Details
A	SER291
B	SER291

---

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

Chain	Residue	Details
A	LYS335
A	LYS343
A	LYS406
B	LYS335
B	LYS343
B	LYS406

---

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	LYS202
B	LYS202

---