Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1TKK

The Structure of a Substrate-Liganded Complex of the L-Ala-D/L-Glu Epimerase from Bacillus subtilis

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0016998	biological_process	cell wall macromolecule catabolic process
A	0046872	molecular_function	metal ion binding
A	0071555	biological_process	cell wall organization
A	0103031	molecular_function	L-Ala-D/L-Glu epimerase activity
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	0016998	biological_process	cell wall macromolecule catabolic process
B	0046872	molecular_function	metal ion binding
B	0071555	biological_process	cell wall organization
B	0103031	molecular_function	L-Ala-D/L-Glu epimerase activity
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	0016998	biological_process	cell wall macromolecule catabolic process
C	0046872	molecular_function	metal ion binding
C	0071555	biological_process	cell wall organization
C	0103031	molecular_function	L-Ala-D/L-Glu epimerase activity
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	0016998	biological_process	cell wall macromolecule catabolic process
D	0046872	molecular_function	metal ion binding
D	0071555	biological_process	cell wall organization
D	0103031	molecular_function	L-Ala-D/L-Glu epimerase activity
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	0016998	biological_process	cell wall macromolecule catabolic process
E	0046872	molecular_function	metal ion binding
E	0071555	biological_process	cell wall organization
E	0103031	molecular_function	L-Ala-D/L-Glu epimerase activity
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	0016998	biological_process	cell wall macromolecule catabolic process
F	0046872	molecular_function	metal ion binding
F	0071555	biological_process	cell wall organization
F	0103031	molecular_function	L-Ala-D/L-Glu epimerase activity
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	0016998	biological_process	cell wall macromolecule catabolic process
G	0046872	molecular_function	metal ion binding
G	0071555	biological_process	cell wall organization
G	0103031	molecular_function	L-Ala-D/L-Glu epimerase activity
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	0016998	biological_process	cell wall macromolecule catabolic process
H	0046872	molecular_function	metal ion binding
H	0071555	biological_process	cell wall organization
H	0103031	molecular_function	L-Ala-D/L-Glu epimerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1601

Chain	Residue
A	LYS160
A	ASP191
A	GLU219
A	ASP244
A	GLU2471
A	HOH2472

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 1602

Chain	Residue
B	ASP244
B	GLU2473
B	HOH2474
B	LYS160
B	ASP191
B	GLU219

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 1603

Chain	Residue
C	LYS160
C	ASP191
C	GLU219
C	ASP244
C	GLU2475
C	HOH2476

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 1604

Chain	Residue
D	ASP191
D	ASN193
D	GLU219
D	ASP244
D	GLU2477
D	HOH2478

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 1605

Chain	Residue
E	ASP191
E	GLU219
E	ASP244
E	GLU2479
E	HOH2480

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 1606

Chain	Residue
F	ASP191
F	GLU219
F	ASP244
F	GLU2481
F	HOH2482

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG G 1607

Chain	Residue
G	LYS160
G	ASP191
G	GLU219
G	ASP244
G	GLU2483
G	HOH2484

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG H 1608

Chain	Residue
H	LYS160
H	ASP191
H	GLU219
H	ASP244
H	GLU2485
H	HOH2486

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ALA A 2470

Chain	Residue
A	PHE19
A	THR135
A	LYS160
A	LYS162
A	ASP321
A	ASP323
A	GLU2471

site_id	BC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GLU A 2471

Chain	Residue
A	PHE19
A	ARG24
A	ILE54
A	LYS160
A	LYS162
A	ASP191
A	ASP244
A	LYS268
A	SER296
A	MET297
A	ILE298
A	MG1601
A	ALA2470
A	HOH2541
A	HOH2577

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ALA B 2472

Chain	Residue
B	PHE19
B	THR135
B	LYS160
B	LYS162
B	ASP321
B	ASP323
B	GLU2473

site_id	BC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GLU B 2473

Chain	Residue
B	PHE19
B	ARG24
B	ILE54
B	LYS160
B	LYS162
B	ASP191
B	GLU219
B	ASP244
B	LYS268
B	SER296
B	ILE298
B	MG1602
B	ALA2472
B	HOH2484
B	HOH2510

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ALA C 2474

Chain	Residue
C	THR135
C	LYS160
C	LYS162
C	ASP321
C	ASP323
C	GLU2475

site_id	BC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GLU C 2475

Chain	Residue
C	LYS160
C	LYS162
C	ASP191
C	ASP244
C	LYS268
C	SER296
C	MET297
C	ILE298
C	MG1603
C	ALA2474
C	HOH2479
C	PHE19
C	ARG24
C	ILE54

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ALA D 2476

Chain	Residue
D	PHE19
D	THR135
D	LYS160
D	LYS162
D	ASP321
D	ASP323
D	GLU2477

site_id	BC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GLU D 2477

Chain	Residue
D	PHE19
D	ARG24
D	ILE54
D	LYS160
D	LYS162
D	ASP191
D	ASP244
D	LYS268
D	SER296
D	MET297
D	ILE298
D	MG1604
D	ALA2476
D	HOH2521
D	HOH2530

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ALA E 2478

Chain	Residue
E	THR135
E	LYS160
E	LYS162
E	ASP321
E	ASP323
E	GLU2479

site_id	BC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GLU E 2479

Chain	Residue
E	PHE19
E	ARG24
E	LYS160
E	LYS162
E	ASP244
E	LYS268
E	SER296
E	ILE298
E	MG1605
E	ALA2478
E	HOH2526
E	HOH2528

site_id	CC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ALA F 2480

Chain	Residue
F	PHE19
F	THR135
F	LYS160
F	LYS162
F	ASP321
F	ASP323
F	GLU2481

site_id	CC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GLU F 2481

Chain	Residue
F	PHE19
F	ARG24
F	ILE54
F	LYS160
F	LYS162
F	ASP191
F	ASP244
F	LYS268
F	SER296
F	MET297
F	ILE298
F	MG1606
F	ALA2480
F	HOH2531
F	HOH2539

site_id	CC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ALA G 2482

Chain	Residue
G	PHE19
G	THR135
G	LYS160
G	LYS162
G	SER296
G	ASP321
G	ASP323
G	GLU2483

site_id	CC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GLU G 2483

Chain	Residue
G	PHE19
G	ARG24
G	ILE54
G	LYS160
G	LYS162
G	ASP191
G	ASP244
G	LYS268
G	SER296
G	MET297
G	ILE298
G	MG1607
G	ALA2482
G	HOH2519
G	HOH2520

site_id	CC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ALA H 2484

Chain	Residue
H	PHE19
H	THR135
H	LYS160
H	LYS162
H	ASP321
H	ASP323
H	GLU2485

site_id	CC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GLU H 2485

Chain	Residue
H	ARG24
H	ILE54
H	LYS160
H	LYS162
H	ASP191
H	ASP244
H	LYS268
H	SER296
H	MET297
H	ILE298
H	MG1608
H	ALA2484
H	HOH2493
H	HOH2550

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor; specific for (R)-substrate epimerization => ECO:0000269\|PubMed:15301535

Chain	Residue	Details
A	LYS162
B	LYS162
C	LYS162
D	LYS162
E	LYS162
F	LYS162
G	LYS162
H	LYS162

site_id	SWS_FT_FI2
Number of Residues	8
Details	ACT_SITE: Proton acceptor; specific for (S)-substrate epimerization => ECO:0000269\|PubMed:15301535

Chain	Residue	Details
A	LYS268
B	LYS268
C	LYS268
D	LYS268
E	LYS268
F	LYS268
G	LYS268
H	LYS268

site_id	SWS_FT_FI3
Number of Residues	56
Details	BINDING: BINDING => ECO:0000269\|PubMed:15301535

Chain	Residue	Details
D	SER296
D	ILE298
D	ASP321
D	ASP323
E	ARG24
E	THR135
E	LYS160
E	SER296
E	ILE298
E	ASP321
E	ASP323
F	ARG24
F	THR135
F	LYS160
F	SER296
F	ILE298
F	ASP321
F	ASP323
G	ARG24
G	THR135
G	LYS160
G	SER296
G	ILE298
G	ASP321
G	ASP323
H	ARG24
H	THR135
H	LYS160
H	SER296
H	ILE298
H	ASP321
H	ASP323
A	SER296
A	ILE298
A	ASP321
A	ASP323
B	ARG24
B	THR135
B	LYS160
B	SER296
B	ILE298
B	ASP321
B	ASP323
C	ARG24
C	THR135
C	LYS160
C	SER296
C	ILE298
C	ASP321
C	ASP323
D	ARG24
D	THR135
D	LYS160
A	ARG24
A	THR135
A	LYS160

site_id	SWS_FT_FI4
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:11747448, ECO:0000269\|PubMed:15301535

Chain	Residue	Details
A	GLU219
A	ASP244
B	ASP191
B	GLU219
B	ASP244
C	ASP191
C	GLU219
C	ASP244
D	ASP191
D	GLU219
D	ASP244
E	ASP191
E	GLU219
E	ASP244
F	ASP191
F	GLU219
F	ASP244
G	ASP191
G	GLU219
G	ASP244
H	ASP191
H	GLU219
H	ASP244
A	ASP191

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 957

Chain	Residue	Details
A	LYS162	proton acceptor, proton donor
A	ASP191	metal ligand
A	GLU219	metal ligand
A	ASP244	metal ligand
A	LYS268	proton acceptor, proton donor

site_id	MCSA2
Number of Residues	5
Details	M-CSA 957

Chain	Residue	Details
B	LYS162	proton acceptor, proton donor
B	ASP191	metal ligand
B	GLU219	metal ligand
B	ASP244	metal ligand
B	LYS268	proton acceptor, proton donor

site_id	MCSA3
Number of Residues	5
Details	M-CSA 957

Chain	Residue	Details
C	LYS162	proton acceptor, proton donor
C	ASP191	metal ligand
C	GLU219	metal ligand
C	ASP244	metal ligand
C	LYS268	proton acceptor, proton donor

site_id	MCSA4
Number of Residues	5
Details	M-CSA 957

Chain	Residue	Details
D	LYS162	proton acceptor, proton donor
D	ASP191	metal ligand
D	GLU219	metal ligand
D	ASP244	metal ligand
D	LYS268	proton acceptor, proton donor

site_id	MCSA5
Number of Residues	5
Details	M-CSA 957

Chain	Residue	Details
E	LYS162	proton acceptor, proton donor
E	ASP191	metal ligand
E	GLU219	metal ligand
E	ASP244	metal ligand
E	LYS268	proton acceptor, proton donor

site_id	MCSA6
Number of Residues	5
Details	M-CSA 957

Chain	Residue	Details
F	LYS162	proton acceptor, proton donor
F	ASP191	metal ligand
F	GLU219	metal ligand
F	ASP244	metal ligand
F	LYS268	proton acceptor, proton donor

site_id	MCSA7
Number of Residues	5
Details	M-CSA 957

Chain	Residue	Details
G	LYS162	proton acceptor, proton donor
G	ASP191	metal ligand
G	GLU219	metal ligand
G	ASP244	metal ligand
G	LYS268	proton acceptor, proton donor

site_id	MCSA8
Number of Residues	5
Details	M-CSA 957

Chain	Residue	Details
H	LYS162	proton acceptor, proton donor
H	ASP191	metal ligand
H	GLU219	metal ligand
H	ASP244	metal ligand
H	LYS268	proton acceptor, proton donor

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