Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3JW7

Crystal structure of Dipeptide Epimerase from Enterococcus faecalis V583 complexed with Mg and dipeptide L-Ile-L-Tyr

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0006518	biological_process	peptide metabolic process
A	0009063	biological_process	amino acid catabolic process
A	0016853	molecular_function	isomerase activity
A	0016854	molecular_function	racemase and epimerase activity
A	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0006518	biological_process	peptide metabolic process
B	0009063	biological_process	amino acid catabolic process
B	0016853	molecular_function	isomerase activity
B	0016854	molecular_function	racemase and epimerase activity
B	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0006518	biological_process	peptide metabolic process
C	0009063	biological_process	amino acid catabolic process
C	0016853	molecular_function	isomerase activity
C	0016854	molecular_function	racemase and epimerase activity
C	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0006518	biological_process	peptide metabolic process
D	0009063	biological_process	amino acid catabolic process
D	0016853	molecular_function	isomerase activity
D	0016854	molecular_function	racemase and epimerase activity
D	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
D	0046872	molecular_function	metal ion binding
E	0000287	molecular_function	magnesium ion binding
E	0006518	biological_process	peptide metabolic process
E	0009063	biological_process	amino acid catabolic process
E	0016853	molecular_function	isomerase activity
E	0016854	molecular_function	racemase and epimerase activity
E	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
E	0046872	molecular_function	metal ion binding
F	0000287	molecular_function	magnesium ion binding
F	0006518	biological_process	peptide metabolic process
F	0009063	biological_process	amino acid catabolic process
F	0016853	molecular_function	isomerase activity
F	0016854	molecular_function	racemase and epimerase activity
F	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
F	0046872	molecular_function	metal ion binding
G	0000287	molecular_function	magnesium ion binding
G	0006518	biological_process	peptide metabolic process
G	0009063	biological_process	amino acid catabolic process
G	0016853	molecular_function	isomerase activity
G	0016854	molecular_function	racemase and epimerase activity
G	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
G	0046872	molecular_function	metal ion binding
H	0000287	molecular_function	magnesium ion binding
H	0006518	biological_process	peptide metabolic process
H	0009063	biological_process	amino acid catabolic process
H	0016853	molecular_function	isomerase activity
H	0016854	molecular_function	racemase and epimerase activity
H	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ILE A 355

Chain	Residue
A	PHE19
A	THR134
A	LYS161
A	CYS292
A	ASP318
A	ASP320
A	TYR356

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TYR A 356

Chain	Residue
A	PHE53
A	LYS159
A	LYS161
A	ASP189
A	ASN191
A	ASP240
A	LYS264
A	CYS292
A	ALA294
A	GLU295
A	ILE355
A	MG358
A	HOH369
A	ILE21
A	ILE26

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 357

Chain	Residue
A	LEU15
A	PHE19
A	ASP320
A	ALA321
A	PHE323
A	GLY324
A	HOH449
A	HOH1068
A	HOH1258

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 358

Chain	Residue
A	LYS159
A	ASP189
A	GLU215
A	ASP240
A	TYR356
A	HOH360

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ILE B 355

Chain	Residue
B	PHE19
B	THR134
B	LYS159
B	LYS161
B	CYS292
B	ASP318
B	ASP320
B	TYR356

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TYR B 356

Chain	Residue
B	ILE21
B	ILE26
B	PHE53
B	LYS159
B	LYS161
B	ASP189
B	ASN191
B	ASP240
B	LYS264
B	CYS292
B	ALA294
B	GLU295
B	ILE355
B	MG358
B	HOH369

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 357

Chain	Residue
B	LEU15
B	PHE19
B	ASP320
B	ALA321
B	GLY324
B	HOH644
B	HOH1030
B	HOH1082

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 358

Chain	Residue
B	LYS159
B	ASP189
B	GLU215
B	ASP240
B	TYR356
B	HOH359

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ILE C 355

Chain	Residue
C	PHE19
C	THR134
C	LYS161
C	CYS292
C	ASP318
C	ASP320
C	TYR356

site_id	BC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE TYR C 356

Chain	Residue
C	ILE21
C	PHE53
C	LYS159
C	LYS161
C	ASP189
C	ASN191
C	ASP240
C	LYS264
C	CYS292
C	ALA294
C	GLU295
C	ILE355
C	MG358
C	HOH364

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 357

Chain	Residue
C	PHE323
C	GLY324
C	HOH864
C	LEU15
C	PHE19
C	ASP320
C	ALA321

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 358

Chain	Residue
C	LYS159
C	ASP189
C	GLU215
C	ASP240
C	TYR356
C	HOH363

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ILE D 355

Chain	Residue
D	THR134
D	LYS161
D	CYS292
D	ASP318
D	ASP320
D	TYR356

site_id	BC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TYR D 356

Chain	Residue
D	ILE21
D	ILE26
D	PHE53
D	LYS159
D	LYS161
D	ASP189
D	ASN191
D	ASP240
D	LYS264
D	CYS292
D	ALA294
D	GLU295
D	ILE355
D	MG358
D	HOH397

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 357

Chain	Residue
D	LEU15
D	PHE19
D	THR134
D	ASP320
D	ALA321
D	GLY324
D	HOH519

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 358

Chain	Residue
D	LYS159
D	ASP189
D	GLU215
D	ASP240
D	TYR356
D	HOH925

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ILE E 355

Chain	Residue
E	THR134
E	LYS159
E	LYS161
E	CYS292
E	ASP318
E	ASP320
E	TYR356

site_id	BC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TYR E 356

Chain	Residue
E	ILE26
E	PHE53
E	LYS159
E	LYS161
E	ASP189
E	ASN191
E	GLU215
E	ASP240
E	LYS264
E	CYS292
E	ALA294
E	GLU295
E	ILE355
E	MG358
E	HOH387

site_id	CC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL E 357

Chain	Residue
E	LEU15
E	PHE19
E	ASP320
E	ALA321
E	GLY324
E	HOH414
E	HOH459

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 358

Chain	Residue
E	LYS159
E	ASP189
E	GLU215
E	ASP240
E	TYR356
E	HOH368

site_id	CC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ILE F 355

Chain	Residue
F	THR134
F	LYS159
F	LYS161
F	CYS292
F	ASP318
F	ASP320
F	TYR356

site_id	CC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TYR F 356

Chain	Residue
F	ILE21
F	PHE53
F	LYS159
F	LYS161
F	ASP189
F	ASN191
F	GLU215
F	ASP240
F	LYS264
F	CYS292
F	ALA294
F	GLU295
F	ILE355
F	MG358
F	HOH390

site_id	CC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL F 357

Chain	Residue
F	LEU15
F	PHE19
F	ASP320
F	ALA321
F	PHE323
F	GLY324
F	HOH808
F	HOH1032
F	HOH2157

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 358

Chain	Residue
F	ASP189
F	GLU215
F	ASP240
F	TYR356
F	HOH393

site_id	CC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ILE G 355

Chain	Residue
G	THR134
G	LYS159
G	LYS161
G	CYS292
G	ASP318
G	ASP320
G	TYR356

site_id	CC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TYR G 356

Chain	Residue
G	ILE21
G	ILE26
G	PHE53
G	LYS159
G	LYS161
G	ASP189
G	ASN191
G	ASP240
G	LYS264
G	CYS292
G	ALA294
G	GLU295
G	ILE355
G	MG358
G	HOH406

site_id	CC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL G 357

Chain	Residue
G	LEU15
G	PHE19
G	ASP320
G	ALA321
G	GLY324
G	HOH719
G	HOH1047
G	HOH2223

site_id	DC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG G 358

Chain	Residue
G	ASP189
G	GLU215
G	ASP240
G	TYR356
G	HOH384

site_id	DC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ILE H 355

Chain	Residue
H	THR134
H	LYS159
H	LYS161
H	CYS292
H	ASP318
H	ASP320
H	TYR356

site_id	DC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TYR H 356

Chain	Residue
H	ILE26
H	PHE53
H	LYS159
H	LYS161
H	ASP189
H	ASN191
H	GLU215
H	ASP240
H	LYS264
H	CYS292
H	ALA294
H	GLU295
H	ILE355
H	MG358
H	HOH417

site_id	DC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL H 357

Chain	Residue
H	LEU15
H	PHE19
H	ASP320
H	ALA321
H	PHE323
H	GLY324
H	HOH406
H	HOH788
H	HOH797

site_id	DC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG H 358

Chain	Residue
H	LYS159
H	ASP189
H	GLU215
H	ASP240
H	TYR356
H	HOH359

Functional Information from PROSITE/UniProt

site_id	PS00909
Number of Residues	32
Details	MR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. LrlDaNqawtpkdAvkaiqaLadyqielVEQP

Chain	Residue	Details
A	LEU186-PRO217

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	72
Details	BINDING:

Chain	Residue	Details
A	THR134
B	THR134
B	LYS159
B	ASP189
B	ASN191
B	GLU215
B	ASP240
B	LYS264
B	CYS292
B	ASP318
C	THR134
A	LYS159
C	LYS159
C	ASP189
C	ASN191
C	GLU215
C	ASP240
C	LYS264
C	CYS292
C	ASP318
D	THR134
D	LYS159
A	ASP189
D	ASP189
D	ASN191
D	GLU215
D	ASP240
D	LYS264
D	CYS292
D	ASP318
E	THR134
E	LYS159
E	ASP189
A	ASN191
E	ASN191
E	GLU215
E	ASP240
E	LYS264
E	CYS292
E	ASP318
F	THR134
F	LYS159
F	ASP189
F	ASN191
A	GLU215
F	GLU215
F	ASP240
F	LYS264
F	CYS292
F	ASP318
G	THR134
G	LYS159
G	ASP189
G	ASN191
G	GLU215
A	ASP240
G	ASP240
G	LYS264
G	CYS292
G	ASP318
H	THR134
H	LYS159
H	ASP189
H	ASN191
H	GLU215
H	ASP240
A	LYS264
H	LYS264
H	CYS292
H	ASP318
A	CYS292
A	ASP318

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