Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2QUV

Phosphate ions in fructose-1,6-bisphosphate aldolase from rabbit muscle

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004332	molecular_function	fructose-bisphosphate aldolase activity
A	0005515	molecular_function	protein binding
A	0006096	biological_process	glycolytic process
A	0016829	molecular_function	lyase activity
A	0030335	biological_process	positive regulation of cell migration
A	0031430	cellular_component	M band
A	0031674	cellular_component	I band
A	0034316	biological_process	negative regulation of Arp2/3 complex-mediated actin nucleation
A	0051289	biological_process	protein homotetramerization
B	0004332	molecular_function	fructose-bisphosphate aldolase activity
B	0005515	molecular_function	protein binding
B	0006096	biological_process	glycolytic process
B	0016829	molecular_function	lyase activity
B	0030335	biological_process	positive regulation of cell migration
B	0031430	cellular_component	M band
B	0031674	cellular_component	I band
B	0034316	biological_process	negative regulation of Arp2/3 complex-mediated actin nucleation
B	0051289	biological_process	protein homotetramerization
C	0004332	molecular_function	fructose-bisphosphate aldolase activity
C	0005515	molecular_function	protein binding
C	0006096	biological_process	glycolytic process
C	0016829	molecular_function	lyase activity
C	0030335	biological_process	positive regulation of cell migration
C	0031430	cellular_component	M band
C	0031674	cellular_component	I band
C	0034316	biological_process	negative regulation of Arp2/3 complex-mediated actin nucleation
C	0051289	biological_process	protein homotetramerization
D	0004332	molecular_function	fructose-bisphosphate aldolase activity
D	0005515	molecular_function	protein binding
D	0006096	biological_process	glycolytic process
D	0016829	molecular_function	lyase activity
D	0030335	biological_process	positive regulation of cell migration
D	0031430	cellular_component	M band
D	0031674	cellular_component	I band
D	0034316	biological_process	negative regulation of Arp2/3 complex-mediated actin nucleation
D	0051289	biological_process	protein homotetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 A 3001

Chain	Residue
A	SER271
A	HOH3317
A	HOH3507
A	GLY272
A	GLY273
A	GLY302
A	ARG303
A	HOH3005
A	HOH3068
A	HOH3150
A	HOH3315

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 3002

Chain	Residue
B	LEU270
B	SER271
B	GLY272
B	SER300
B	GLY302
B	HOH3319
B	HOH3448

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 B 3003

Chain	Residue
B	SER271
B	GLY273
B	GLY302
B	ARG303
B	HOH3012
B	HOH3013
B	HOH3014
B	HOH3028
B	HOH3307

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 3007

Chain	Residue
B	GLN202
B	THR254
B	ARG258
B	HOH3034
B	HOH3283
C	LYS12
C	HOH3059

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 C 3004

Chain	Residue
C	SER271
C	GLY302
C	ARG303
C	HOH3146
C	HOH3357
C	HOH3380
C	HOH3445
C	HOH3454
C	HOH3524
C	HOH3551

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 D 3005

Chain	Residue
D	SER271
D	GLY272
D	GLY302
D	ARG303
D	HOH3047
D	HOH3145
D	HOH3337
D	HOH3510

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 D 3006

Chain	Residue
A	LYS12
D	GLN202
D	THR254
D	ARG258
D	HOH3057
D	HOH3474

Functional Information from PROSITE/UniProt

site_id	PS00158
Number of Residues	11
Details	ALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. IyLEGtLLKPN

Chain	Residue	Details
A	ILE221-ASN231

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11779856","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Schiff-base intermediate with dihydroxyacetone-P","evidences":[{"source":"PubMed","id":"11779856","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10504235","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6ALD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Site: {"description":"Essential for substrate cleavage"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Site: {"description":"Alkylation inactivates the enzyme"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Site: {"description":"Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Site: {"description":"Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	16
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	8
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Modified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P05065","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	4
Details	Modified residue: {"description":"Deamidated asparagine; in form beta","evidences":[{"source":"PubMed","id":"4857186","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ald

Chain	Residue	Details
A	GLU187
A	LYS229
A	ASP33

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1ald

Chain	Residue	Details
B	GLU187
B	LYS229
B	ASP33

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ald

Chain	Residue	Details
C	GLU187
C	LYS229
C	ASP33

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ald

Chain	Residue	Details
D	GLU187
D	LYS229
D	ASP33

site_id	MCSA1
Number of Residues	7
Details	M-CSA 222

Chain	Residue	Details
A	ASP33	electrostatic stabiliser, hydrogen bond acceptor
A	LYS146	electrostatic stabiliser, hydrogen bond donor
A	GLU187	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay
A	GLU189	activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction
A	LYS229	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay
A	SER300	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	TYR363	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	7
Details	M-CSA 222

Chain	Residue	Details
B	ASP33	electrostatic stabiliser, hydrogen bond acceptor
B	LYS146	electrostatic stabiliser, hydrogen bond donor
B	GLU187	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay
B	GLU189	activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction
B	LYS229	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay
B	SER300	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
B	TYR363	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	7
Details	M-CSA 222

Chain	Residue	Details
C	ASP33	electrostatic stabiliser, hydrogen bond acceptor
C	LYS146	electrostatic stabiliser, hydrogen bond donor
C	GLU187	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay
C	GLU189	activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction
C	LYS229	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay
C	SER300	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
C	TYR363	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA4
Number of Residues	7
Details	M-CSA 222

Chain	Residue	Details
D	ASP33	electrostatic stabiliser, hydrogen bond acceptor
D	LYS146	electrostatic stabiliser, hydrogen bond donor
D	GLU187	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay
D	GLU189	activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction
D	LYS229	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay
D	SER300	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
D	TYR363	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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