Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1B57

CLASS II FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE IN COMPLEX WITH PHOSPHOGLYCOLOHYDROXAMATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004332	molecular_function	fructose-bisphosphate aldolase activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0008270	molecular_function	zinc ion binding
A	0016829	molecular_function	lyase activity
A	0016832	molecular_function	aldehyde-lyase activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
B	0004332	molecular_function	fructose-bisphosphate aldolase activity
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0008270	molecular_function	zinc ion binding
B	0016829	molecular_function	lyase activity
B	0016832	molecular_function	aldehyde-lyase activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 360

Chain	Residue
A	HIS110
A	HIS226
A	HIS264
A	PGH359

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 361

Chain	Residue
A	ASP144
A	SER146
A	GLU174
A	GLU181
A	HOH448

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 362

Chain	Residue
A	HIS91
A	HIS129
A	HOH437
A	HOH439

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 363

Chain	Residue
A	SER1
A	CL365
B	GLU246
B	HIS256

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 364

Chain	Residue
A	VAL225
A	GLY227
A	GLY265
A	SER267
A	PGH359
A	HOH390

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 365

Chain	Residue
A	SER1
A	ZN363
B	GLU246
B	HIS256

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 360

Chain	Residue
B	HIS110
B	HIS226
B	HIS264
B	PGH359

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 361

Chain	Residue
B	ASP144
B	SER146
B	GLU174
B	GLU181
B	HOH392

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 362

Chain	Residue
B	HIS91
B	HIS129
B	HOH423
B	HOH424

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA B 364

Chain	Residue
B	VAL225
B	GLY227
B	GLY265
B	SER267
B	PGH359
B	HOH414

site_id	BC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PGH A 359

Chain	Residue
A	ASP109
A	HIS110
A	HIS226
A	GLY227
A	HIS264
A	GLY265
A	GLY266
A	SER267
A	ASN286
A	ILE287
A	ASP288
A	THR289
A	ZN360
A	NA364
A	HOH394
A	HOH395

site_id	BC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PGH B 359

Chain	Residue
B	ASP109
B	HIS110
B	VAL225
B	HIS226
B	GLY227
B	HIS264
B	GLY265
B	SER267
B	ASN286
B	ILE287
B	ASP288
B	THR289
B	ZN360
B	NA364
B	HOH383
B	HOH384

Functional Information from PROSITE/UniProt

site_id	PS00602
Number of Residues	12
Details	ALDOLASE_CLASS_II_1 Fructose-bisphosphate aldolase class-II signature 1. Yg..VPVi.LHtDHC

Chain	Residue	Details
A	TYR100-CYS111

site_id	PS00806
Number of Residues	12
Details	ALDOLASE_CLASS_II_2 Fructose-bisphosphate aldolase class-II signature 2. LEiELGctGGeE

Chain	Residue	Details
A	LEU171-GLU182

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000269\|PubMed:10080900

Chain	Residue	Details
A	HIS110
B	HIS110

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	ASN62
B	ASN62

site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269\|PubMed:10080900, ECO:0000269\|PubMed:8836102, ECO:0000269\|PubMed:8939754

Chain	Residue	Details
A	CYS111
B	GLY265
A	LEU145
A	LEU175
A	GLY227
A	GLY265
B	CYS111
B	LEU145
B	LEU175
B	GLY227

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING:

Chain	Residue	Details
A	VAL228
A	GLY266
A	ILE287
B	VAL228
B	GLY266
B	ILE287

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:21151122

Chain	Residue	Details
A	PRO9
B	PRO9

site_id	SWS_FT_FI6
Number of Residues	14
Details	MOD_RES: N6-succinyllysine => ECO:0000269\|PubMed:21151122

Chain	Residue	Details
A	GLY72
B	PRO231
B	LYS251
B	GLY319
B	LYS326
B	ALA348
A	LEU115
A	PRO231
A	LYS251
A	GLY319
A	LYS326
A	ALA348
B	GLY72
B	LEU115

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 52

Chain	Residue	Details
A	HIS110	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	CYS111	metal ligand
A	ASP183	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLY227	metal ligand
A	GLY265	metal ligand
A	ILE287	electrostatic stabiliser, hydrogen bond donor, steric role

site_id	MCSA2
Number of Residues	6
Details	M-CSA 52

Chain	Residue	Details
B	HIS110	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	CYS111	metal ligand
B	ASP183	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLY227	metal ligand
B	GLY265	metal ligand
B	ILE287	electrostatic stabiliser, hydrogen bond donor, steric role

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