Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4GYP

Crystal structure of the heterotetrameric complex of GlucD and GlucDRP from E. coli K-12 MG1655 (EFI TARGET EFI-506058)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0008872	molecular_function	glucarate dehydratase activity
A	0016829	molecular_function	lyase activity
A	0019394	biological_process	glucarate catabolic process
A	0042838	biological_process	D-glucarate catabolic process
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0008872	molecular_function	glucarate dehydratase activity
B	0016829	molecular_function	lyase activity
B	0019394	biological_process	glucarate catabolic process
B	0042838	biological_process	D-glucarate catabolic process
B	0046872	molecular_function	metal ion binding
C	0009063	biological_process	amino acid catabolic process
C	0016829	molecular_function	lyase activity
C	0044248	biological_process	cellular catabolic process
C	0046872	molecular_function	metal ion binding
D	0009063	biological_process	amino acid catabolic process
D	0016829	molecular_function	lyase activity
D	0044248	biological_process	cellular catabolic process
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 501

Chain	Residue
A	ASP235
A	ASN237
A	GLU260
A	ASP261
A	ASN289

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 A 502

Chain	Residue
A	ASN341
A	HIS368
A	ARG422
A	HOH601
A	HOH610
A	HOH613
A	ASN27
A	HIS32
A	PHE152
A	LYS207

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 503

Chain	Residue
A	GLY299
A	SER303
A	HOH832
A	HOH995
B	LEU302
B	GLN305
B	PHE332
D	ARG279

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PEG A 504

Chain	Residue
A	HIS49
A	GLN126
A	HIS127
A	GLY129
A	HOH617
A	HOH719
A	HOH924
B	PHE5
D	GLY169
D	ASN170

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 501

Chain	Residue
B	ASP235
B	ASN237
B	GLU260
B	ASP261
B	ASN289

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 B 502

Chain	Residue
B	ASN27
B	HIS32
B	PHE152
B	LYS207
B	ASN341
B	HIS368
B	ARG422
B	HOH604
B	HOH672
B	HOH678

site_id	AC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CIT C 501

Chain	Residue
C	ASN26
C	ILE27
C	HIS31
C	LYS206
C	ASN236
C	HIS338
C	ASN340
C	HIS367
C	ARG421
C	HOH667
C	HOH728
C	HOH874
C	HOH910

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 502

Chain	Residue
A	LEU302
A	PHE332
A	HOH995
B	GLY299
B	SER303
C	ARG279
C	HOH680
C	HOH814

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG C 503

Chain	Residue
C	ASN80
C	HOH940
D	ASN80
D	LEU123

site_id	BC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CIT D 501

Chain	Residue
D	ASN26
D	ILE27
D	HIS31
D	TRP103
D	PHE105
D	PHE151
D	LYS206
D	ASN236
D	HIS338
D	ASN340
D	HIS367
D	ARG421
D	HOH629
D	HOH694
D	HOH733

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE P6G D 502

Chain	Residue
B	GLY283
B	PRO285
B	ASP308
D	ARG279
D	GLY282
D	PRO284
D	ASP307
D	HOH604
D	HOH758

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 503

Chain	Residue
D	SER319
D	ARG323
D	HOH606
D	HOH639
C	HOH685
D	THR317

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 504

Chain	Residue
A	GLN391
A	HOH731
A	HOH925
A	HOH926
D	ARG376
D	ASP402
D	GLU404
D	GLN405
D	LYS408

site_id	BC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PEG D 505

Chain	Residue
D	ASN360

Functional Information from PROSITE/UniProt

site_id	PS00908
Number of Residues	26
Details	MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AvAALEaALlDLlGKalnvPVceLLG

Chain	Residue	Details
C	ALA111-GLY136

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255

Chain	Residue	Details
C	LYS206
C	HIS338
D	LYS206
D	HIS338

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
C	HIS31
D	THR104
D	TYR149
D	LYS204
D	ASN288
D	HIS338
D	HIS367
D	ARG421
C	THR104
C	TYR149
C	LYS204
C	ASN288
C	HIS338
C	HIS367
C	ARG421
D	HIS31

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255

Chain	Residue	Details
C	ASP234
C	GLU265
D	ASP234
D	GLU265

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	9
Details	M-CSA 451

Chain	Residue	Details
A	LYS205	electrostatic stabiliser
A	LYS207	electrostatic stabiliser
A	ASP235	metal ligand
A	ASN237	activator, electrostatic stabiliser
A	GLU260	metal ligand
A	ASN289	metal ligand
A	ASP313	electrostatic stabiliser, modifies pKa
A	HIS339	proton acceptor, proton donor
A	ASN341	activator

site_id	MCSA2
Number of Residues	9
Details	M-CSA 451

Chain	Residue	Details
B	LYS205	electrostatic stabiliser
B	LYS207	electrostatic stabiliser
B	ASP235	metal ligand
B	ASN237	activator, electrostatic stabiliser
B	GLU260	metal ligand
B	ASN289	metal ligand
B	ASP313	electrostatic stabiliser, modifies pKa
B	HIS339	proton acceptor, proton donor
B	ASN341	activator

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