6ENL

INHIBITION OF ENOLASE: THE CRYSTAL STRUCTURES OF ENOLASE-CA2+-PHOSPHOGLYCERATE AND ENOLASE-ZN2+-PHOSPHOGLYCOLATE COMPLEXES AT 2.2-ANGSTROMS RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000015	cellular_component	phosphopyruvate hydratase complex
A	0000287	molecular_function	magnesium ion binding
A	0000324	cellular_component	fungal-type vacuole
A	0004634	molecular_function	phosphopyruvate hydratase activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006096	biological_process	glycolytic process
A	0016829	molecular_function	lyase activity
A	0032889	biological_process	regulation of vacuole fusion, non-autophagic
A	0046872	molecular_function	metal ion binding
A	1904408	molecular_function	melatonin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PGA A 442

Chain	Residue
A	GLU168
A	ASP246
A	ASP320
A	LYS345
A	ARG374
A	SER375
A	LYS396
A	ZN438
A	HOH521
A	HOH524
A	HOH611
A	HOH711

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 438

Chain	Residue
A	ASP246
A	GLU295
A	ASP320
A	LYS396
A	PGA442
A	HOH446

---

site_id	CAT
Number of Residues	5
Details	OTHER ACTIVE SITE RESIDUES

Chain	Residue
A	GLU168
A	GLU211
A	LYS345
A	HIS373
A	LYS396

---

site_id	MEI
Number of Residues	3
Details	METAL ION BINDING SITE

Chain	Residue
A	ASP246
A	GLU295
A	ASP320

---

site_id	PHO
Number of Residues	1
Details	PHOSPHATE GROUP BINDING SITE

Chain	Residue
A	ARG374

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU342-SER355

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12846578","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12846578","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8634301","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8605183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9376357","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8605183","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12054465","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8605183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9376357","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00925","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P00925","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P00925","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
A	GLU211
A	HIS373
A	LYS396
A	GLU168

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
A	LYS345
A	GLU211
A	HIS373
A	GLU168

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
A	LYS345
A	HIS191

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
A	LYS242
A	LYS345

---

site_id	MCSA1
Number of Residues	10
Details	M-CSA 311

Chain	Residue	Details
A	SER39	metal ligand
A	LYS396	electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base)
A	HIS159	electrostatic stabiliser, proton shuttle (general acid/base)
A	GLU168	activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction
A	GLU211	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
A	ASP246	metal ligand
A	GLU295	metal ligand
A	ASP320	metal ligand
A	LYS345	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor
A	HIS373	electrostatic stabiliser, hydrogen bond donor

---