Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5TLH

Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 2-naphthol 6-bisphosphonate

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	5
Details	binding site for residue RD2 A 401

Chain	Residue
A	GLU34
A	ARG42
A	SER45
A	ARG303
A	LYS311

site_id	AC2
Number of Residues	9
Details	binding site for residue MDN A 402

Chain	Residue
A	ARG148
A	HOH507
A	HOH518
A	HOH542
A	HOH568
A	ASP33
A	SER38
A	LYS107
A	LYS146

site_id	AC3
Number of Residues	12
Details	binding site for residue GOL B 403

Chain	Residue
A	LEU127
A	GLU165
A	ASN168
A	ARG172
A	HOH504
B	LEU127
B	GLU165
B	ASN168
B	VAL169
B	ARG172
B	HOH501
B	HOH546

site_id	AC4
Number of Residues	6
Details	binding site for residue RD2 B 401

Chain	Residue
B	GLU34
B	ARG42
B	SER45
B	ARG303
B	LYS311
B	HOH503

site_id	AC5
Number of Residues	11
Details	binding site for residue MDN B 402

Chain	Residue
B	ASP33
B	SER35
B	SER38
B	LYS107
B	LYS146
B	ARG148
B	HOH504
B	HOH529
B	HOH591
B	HOH601
B	HOH628

site_id	AC6
Number of Residues	8
Details	binding site for residue RD2 C 401

Chain	Residue
C	GLU34
C	ARG42
C	SER45
C	ARG303
C	LYS311
C	HOH501
C	HOH537
C	HOH572

site_id	AC7
Number of Residues	10
Details	binding site for residue MDN C 402

Chain	Residue
C	SER38
C	LYS107
C	LYS146
C	ARG148
C	HOH503
C	HOH504
C	HOH509
C	HOH552
C	HOH609
C	HOH613

site_id	AC8
Number of Residues	10
Details	binding site for residue GOL D 403

Chain	Residue
C	LEU127
C	GLU165
C	ASN168
C	ARG172
C	HOH576
D	LEU127
D	GLU165
D	ASN168
D	ARG172
D	HOH585

site_id	AC9
Number of Residues	6
Details	binding site for residue RD2 D 401

Chain	Residue
D	GLU34
D	ARG42
D	SER45
D	ARG303
D	LYS311
D	HOH501

site_id	AD1
Number of Residues	7
Details	binding site for residue MDN D 402

Chain	Residue
D	SER38
D	LYS107
D	LYS146
D	ARG148
D	HOH504
D	HOH513
D	HOH545

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	3
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	3
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	3
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	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	6
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

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