Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4H1Z

Crystal structure of putative isomerase from Sinorhizobium meliloti, open loop conformation (target EFI-502104)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0009063	biological_process	amino acid catabolic process
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0009063	biological_process	amino acid catabolic process
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0009063	biological_process	amino acid catabolic process
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0009063	biological_process	amino acid catabolic process
D	0046872	molecular_function	metal ion binding
E	0000287	molecular_function	magnesium ion binding
E	0003824	molecular_function	catalytic activity
E	0009063	biological_process	amino acid catabolic process
E	0046872	molecular_function	metal ion binding
F	0000287	molecular_function	magnesium ion binding
F	0003824	molecular_function	catalytic activity
F	0009063	biological_process	amino acid catabolic process
F	0046872	molecular_function	metal ion binding
G	0000287	molecular_function	magnesium ion binding
G	0003824	molecular_function	catalytic activity
G	0009063	biological_process	amino acid catabolic process
G	0046872	molecular_function	metal ion binding
H	0000287	molecular_function	magnesium ion binding
H	0003824	molecular_function	catalytic activity
H	0009063	biological_process	amino acid catabolic process
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 401

Chain	Residue
A	ASP215
A	GLU241
A	GLU267
A	FMT402
A	HOH517
A	HOH519

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FMT A 402

Chain	Residue
A	GLU267
A	HIS316
A	GLU342
A	GLN344
A	MG401
A	HOH517
A	LYS185
A	ASP215
A	GLU241

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 401

Chain	Residue
B	ASP215
B	GLU241
B	GLU267
B	FMT403
B	HOH504
B	HOH638

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CL B 402

Chain	Residue
B	GLY116
B	GLY117
B	PHE118
B	TYR119
B	HOH687
F	GLY116
F	GLY117
F	PHE118
F	TYR119

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FMT B 403

Chain	Residue
B	TYR21
B	LYS185
B	ASP215
B	GLU241
B	GLU267
B	HIS316
B	GLU342
B	GLN344
B	MG401
B	HOH638

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 404

Chain	Residue
B	THR297
B	MET300
B	ARG301
B	HOH688
B	HOH689

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CL C 401

Chain	Residue
A	GLY116
A	GLY117
A	PHE118
A	TYR119
A	HOH537
C	GLY117
C	PHE118
C	TYR119
C	HOH560

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 402

Chain	Residue
C	ASP215
C	GLU241
C	GLU267
C	FMT404
C	HOH504
C	HOH635

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL C 403

Chain	Residue
C	GLU247
C	ILE249
C	ASP250
D	HOH559

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FMT C 404

Chain	Residue
C	LYS185
C	ASP215
C	GLU241
C	GLU267
C	HIS316
C	GLU342
C	GLN344
C	MG402
C	HOH504

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 401

Chain	Residue
D	ASP215
D	GLU241
D	GLU267
D	HOH515
D	HOH586
D	HOH587

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CL D 402

Chain	Residue
D	GLY116
D	GLY117
D	PHE118
D	TYR119
D	HOH510
H	GLY116
H	PHE118
H	TYR119
H	HOH525

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 401

Chain	Residue
E	ASP215
E	GLU241
E	GLU267
E	FMT402
E	HOH503
E	HOH505

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FMT E 402

Chain	Residue
E	GLU342
E	MG401
E	HOH505
E	LYS185
E	ASP215
E	GLU241
E	GLU267
E	HIS316

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG F 401

Chain	Residue
F	ASP215
F	GLU241
F	GLU267
F	FMT402
F	HOH513
F	HOH612

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FMT F 402

Chain	Residue
F	LYS185
F	ASP215
F	GLU241
F	GLU267
F	HIS316
F	GLU342
F	GLN344
F	MG401
F	HOH612

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL G 401

Chain	Residue
E	GLY117
E	PHE118
E	TYR119
E	HOH536
G	GLY117
G	PHE118

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG G 402

Chain	Residue
G	ASP215
G	GLU241
G	GLU267
G	FMT403
G	HOH507
G	HOH633

site_id	CC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FMT G 403

Chain	Residue
G	LYS185
G	ASP215
G	GLU241
G	GLU267
G	HIS316
G	GLU342
G	GLN344
G	MG402
G	HOH507

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG H 401

Chain	Residue
H	ASP215
H	GLU241
H	GLU267
H	FMT402
H	HOH576
H	HOH615

site_id	CC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FMT H 402

Chain	Residue
H	LYS185
H	ASP215
H	GLU241
H	GLU267
H	HIS316
H	GLU342
H	MG401
H	HOH615

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VDCHEFQHSI

Chain	Residue	Details
A	VAL338-ILE347

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

Chain	Residue	Details
A	ALA122-GLY147

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