Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XH2

Engineering the enolase active site pocket: Crystal structure of the S39N D321A mutant of yeast enolase 1

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	0005515	molecular_function	protein binding
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
B	0000015	cellular_component	phosphopyruvate hydratase complex
B	0000287	molecular_function	magnesium ion binding
B	0000324	cellular_component	fungal-type vacuole
B	0004634	molecular_function	phosphopyruvate hydratase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006096	biological_process	glycolytic process
B	0016829	molecular_function	lyase activity
B	0032889	biological_process	regulation of vacuole fusion, non-autophagic
B	0046872	molecular_function	metal ion binding
B	1904408	molecular_function	melatonin binding
C	0000015	cellular_component	phosphopyruvate hydratase complex
C	0000287	molecular_function	magnesium ion binding
C	0000324	cellular_component	fungal-type vacuole
C	0004634	molecular_function	phosphopyruvate hydratase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006096	biological_process	glycolytic process
C	0016829	molecular_function	lyase activity
C	0032889	biological_process	regulation of vacuole fusion, non-autophagic
C	0046872	molecular_function	metal ion binding
C	1904408	molecular_function	melatonin binding
D	0000015	cellular_component	phosphopyruvate hydratase complex
D	0000287	molecular_function	magnesium ion binding
D	0000324	cellular_component	fungal-type vacuole
D	0004634	molecular_function	phosphopyruvate hydratase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006096	biological_process	glycolytic process
D	0016829	molecular_function	lyase activity
D	0032889	biological_process	regulation of vacuole fusion, non-autophagic
D	0046872	molecular_function	metal ion binding
D	1904408	molecular_function	melatonin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1439

Chain	Residue
A	ASP246
A	GLU295
A	ASP320
A	LYS396
A	2PG1440
A	HOH2497

site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE 2PG A 1440

Chain	Residue
A	GLU211
A	ASP246
A	GLU295
A	ASP320
A	LEU343
A	LYS345
A	HIS373
A	ARG374
A	SER375
A	LYS396
A	MG1439
A	HOH2418
A	HOH2421
A	HOH2456
A	HOH2690
A	HOH2691
A	GLY37
A	ALA38
A	GLU168

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 1439

Chain	Residue
B	ASP246
B	GLU295
B	ASP320
B	HOH2487
B	HOH2618
B	HOH2625

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 2PG B 1440

Chain	Residue
B	GLU211
B	ASP320
B	LYS345
B	ARG374
B	SER375
B	HOH2124
B	HOH2377
B	HOH2616
B	HOH2617
B	HOH2618
B	HOH2619
B	HOH2620
B	HOH2621
B	HOH2622
B	HOH2623
B	HOH2624
B	HOH2625

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 1439

Chain	Residue
C	ASP246
C	GLU295
C	ASP320
C	2PG1440
C	HOH2446

site_id	AC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE 2PG C 1440

Chain	Residue
C	GLY37
C	ALA38
C	GLU168
C	GLU211
C	ASP246
C	GLU295
C	ASP320
C	LEU343
C	LYS345
C	HIS373
C	ARG374
C	SER375
C	LYS396
C	MG1439
C	HOH2383
C	HOH2384
C	HOH2416
C	HOH2623
C	HOH2624

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 1439

Chain	Residue
D	ASP246
D	GLU295
D	ASP320
D	HOH2446
D	HOH2619
D	HOH2620

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 2PG D 1440

Chain	Residue
D	GLU211
D	LYS345
D	ARG374
D	SER375
D	HOH2123
D	HOH2560
D	HOH2618
D	HOH2619
D	HOH2620
D	HOH2621
D	HOH2622
D	HOH2623
D	HOH2624
D	HOH2625
D	HOH2626
D	HOH2627

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	4
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	4
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	20
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	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8605183","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
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	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00925","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P00925","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	8
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	8
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	MCSA1
Number of Residues	10
Details	M-CSA 311

Chain	Residue	Details
A	ASN39	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

site_id	MCSA2
Number of Residues	10
Details	M-CSA 311

Chain	Residue	Details
B	ASN39	metal ligand
B	LYS396	electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base)
B	HIS159	electrostatic stabiliser, proton shuttle (general acid/base)
B	GLU168	activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction
B	GLU211	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
B	ASP246	metal ligand
B	GLU295	metal ligand
B	ASP320	metal ligand
B	LYS345	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor
B	HIS373	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	10
Details	M-CSA 311

Chain	Residue	Details
C	ASN39	metal ligand
C	LYS396	electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base)
C	HIS159	electrostatic stabiliser, proton shuttle (general acid/base)
C	GLU168	activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction
C	GLU211	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
C	ASP246	metal ligand
C	GLU295	metal ligand
C	ASP320	metal ligand
C	LYS345	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor
C	HIS373	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	10
Details	M-CSA 311

Chain	Residue	Details
D	ASN39	metal ligand
D	LYS396	electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base)
D	HIS159	electrostatic stabiliser, proton shuttle (general acid/base)
D	GLU168	activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction
D	GLU211	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
D	ASP246	metal ligand
D	GLU295	metal ligand
D	ASP320	metal ligand
D	LYS345	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor
D	HIS373	electrostatic stabiliser, hydrogen bond donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)