Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1L8P

Mg-phosphonoacetohydroxamate complex of S39A 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	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	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	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	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	5
Details	BINDING SITE FOR RESIDUE MG A 438

Chain	Residue
A	ASP246
A	GLU295
A	ASP320
A	PAH440
A	HOH2011

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 439

Chain	Residue
A	HOH2010
A	PAH440
A	HOH2007
A	HOH2008
A	HOH2009

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 938

Chain	Residue
B	ASP746
B	GLU795
B	ASP820
B	PAH940
B	HOH2016

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 939

Chain	Residue
B	PAH940
B	HOH2012
B	HOH2013
B	HOH2014
B	HOH2015

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 1438

Chain	Residue
C	PAH1440
C	HOH2024
C	HOH2025
C	HOH2026
C	HOH2027

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 1439

Chain	Residue
C	ASP1246
C	GLU1295
C	ASP1320
C	PAH1440
C	HOH2028

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 1938

Chain	Residue
D	PAH1940
D	HOH2019
D	HOH2020
D	HOH2021
D	HOH2022

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 1939

Chain	Residue
D	ASP1746
D	GLU1795
D	ASP1820
D	PAH1940
D	HOH2023

site_id	AC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PAH A 440

Chain	Residue
A	GLY37
A	ALA38
A	GLN167
A	GLU168
A	ASP246
A	GLU295
A	ASP320
A	LEU343
A	LYS345
A	ARG374
A	SER375
A	LYS396
A	MG438
A	MG439
A	HOH2004
A	HOH2007
A	HOH2008
A	HOH2009
A	HOH2853

site_id	BC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PAH B 940

Chain	Residue
B	GLY537
B	ALA538
B	GLN667
B	GLU668
B	ASP746
B	GLU795
B	ASP820
B	LEU843
B	LYS845
B	ARG874
B	SER875
B	LYS896
B	MG938
B	MG939
B	HOH2012
B	HOH2015
B	HOH2018
B	HOH2827

site_id	BC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PAH C 1440

Chain	Residue
C	GLY1037
C	ALA1038
C	GLN1167
C	GLU1168
C	ASP1246
C	GLU1295
C	ASP1320
C	LEU1343
C	LYS1345
C	ARG1374
C	SER1375
C	LYS1396
C	MG1438
C	MG1439
C	HOH2024
C	HOH2025
C	HOH2026
C	HOH2029
C	HOH2603

site_id	BC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PAH D 1940

Chain	Residue
D	GLU1668
D	ASP1746
D	GLU1795
D	ASP1820
D	LEU1843
D	LYS1845
D	ARG1874
D	SER1875
D	LYS1896
D	MG1938
D	MG1939
D	HOH2021
D	HOH2022
D	HOH2382
D	HOH2844
D	GLY1537
D	ALA1538
D	GLN1667

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	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	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
B	HIS691
B	LYS845

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
C	HIS1191
C	LYS1345

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
D	LYS1845
D	HIS1691

site_id	CSA13
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
A	LYS242
A	LYS345

site_id	CSA14
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
B	LYS845
B	LYS742

site_id	CSA15
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
C	LYS1242
C	LYS1345

site_id	CSA16
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
D	LYS1742
D	LYS1845

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

Chain	Residue	Details
B	GLU668
B	LYS896
B	GLU711
B	HIS873

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
C	GLU1211
C	HIS1373
C	GLU1168
C	LYS1396

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
D	HIS1873
D	GLU1668
D	LYS1896
D	GLU1711

site_id	CSA5
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	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
B	GLU668
B	LYS845
B	GLU711
B	HIS873

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
C	GLU1211
C	HIS1373
C	LYS1345
C	GLU1168

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
D	HIS1873
D	GLU1668
D	LYS1845
D	GLU1711

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
A	LYS345
A	HIS191

site_id	MCSA1
Number of Residues	10
Details	M-CSA 311

Chain	Residue	Details
A	ALA39	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	ALA539	metal ligand
B	LYS896	electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base)
B	HIS659	electrostatic stabiliser, proton shuttle (general acid/base)
B	GLU668	activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction
B	GLU711	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
B	ASP746	metal ligand
B	GLU795	metal ligand
B	ASP820	metal ligand
B	LYS845	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor
B	HIS873	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	10
Details	M-CSA 311

Chain	Residue	Details
C	ALA1039	metal ligand
C	LYS1396	electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base)
C	HIS1159	electrostatic stabiliser, proton shuttle (general acid/base)
C	GLU1168	activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction
C	GLU1211	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
C	ASP1246	metal ligand
C	GLU1295	metal ligand
C	ASP1320	metal ligand
C	LYS1345	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor
C	HIS1373	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	10
Details	M-CSA 311

Chain	Residue	Details
D	ALA1539	metal ligand
D	LYS1896	electrostatic stabiliser, hydrogen bond donor, proton shuttle (general acid/base)
D	HIS1659	electrostatic stabiliser, proton shuttle (general acid/base)
D	GLU1668	activator, electrostatic stabiliser, hydrogen bond acceptor, increase acidity, repulsive charge-charge interaction
D	GLU1711	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
D	ASP1746	metal ligand
D	GLU1795	metal ligand
D	ASP1820	metal ligand
D	LYS1845	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor
D	HIS1873	electrostatic stabiliser, hydrogen bond donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)