Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4R1Q

Crystal Structure of Thermophilic Geobacillus kaustophilus L-Arabinose isomerase in complex with L-arabitol

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005996	biological_process	monosaccharide metabolic process
A	0008733	molecular_function	L-arabinose isomerase activity
A	0016853	molecular_function	isomerase activity
A	0016861	molecular_function	intramolecular oxidoreductase activity, interconverting aldoses and ketoses
A	0019568	biological_process	arabinose catabolic process
A	0019569	biological_process	L-arabinose catabolic process to D-xylulose 5-phosphate
A	0030145	molecular_function	manganese ion binding
A	0046872	molecular_function	metal ion binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005996	biological_process	monosaccharide metabolic process
B	0008733	molecular_function	L-arabinose isomerase activity
B	0016853	molecular_function	isomerase activity
B	0016861	molecular_function	intramolecular oxidoreductase activity, interconverting aldoses and ketoses
B	0019568	biological_process	arabinose catabolic process
B	0019569	biological_process	L-arabinose catabolic process to D-xylulose 5-phosphate
B	0030145	molecular_function	manganese ion binding
B	0046872	molecular_function	metal ion binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005996	biological_process	monosaccharide metabolic process
C	0008733	molecular_function	L-arabinose isomerase activity
C	0016853	molecular_function	isomerase activity
C	0016861	molecular_function	intramolecular oxidoreductase activity, interconverting aldoses and ketoses
C	0019568	biological_process	arabinose catabolic process
C	0019569	biological_process	L-arabinose catabolic process to D-xylulose 5-phosphate
C	0030145	molecular_function	manganese ion binding
C	0046872	molecular_function	metal ion binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005996	biological_process	monosaccharide metabolic process
D	0008733	molecular_function	L-arabinose isomerase activity
D	0016853	molecular_function	isomerase activity
D	0016861	molecular_function	intramolecular oxidoreductase activity, interconverting aldoses and ketoses
D	0019568	biological_process	arabinose catabolic process
D	0019569	biological_process	L-arabinose catabolic process to D-xylulose 5-phosphate
D	0030145	molecular_function	manganese ion binding
D	0046872	molecular_function	metal ion binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005996	biological_process	monosaccharide metabolic process
E	0008733	molecular_function	L-arabinose isomerase activity
E	0016853	molecular_function	isomerase activity
E	0016861	molecular_function	intramolecular oxidoreductase activity, interconverting aldoses and ketoses
E	0019568	biological_process	arabinose catabolic process
E	0019569	biological_process	L-arabinose catabolic process to D-xylulose 5-phosphate
E	0030145	molecular_function	manganese ion binding
E	0046872	molecular_function	metal ion binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005996	biological_process	monosaccharide metabolic process
F	0008733	molecular_function	L-arabinose isomerase activity
F	0016853	molecular_function	isomerase activity
F	0016861	molecular_function	intramolecular oxidoreductase activity, interconverting aldoses and ketoses
F	0019568	biological_process	arabinose catabolic process
F	0019569	biological_process	L-arabinose catabolic process to D-xylulose 5-phosphate
F	0030145	molecular_function	manganese ion binding
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE SST A 501

Chain	Residue
A	MET186
A	HOH631
E	GLN17
E	LEU19
E	TYR20
E	PHE84
E	GLN126
E	HIS129
E	HOH624
A	GLU307
A	GLU332
A	HIS349
A	MET350
A	ILE371
A	HIS447
A	HIS448
A	MN503

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE SST A 502

Chain	Residue
A	GLN17
A	LEU19
A	TYR20
A	PHE84
A	GLN126
A	HIS129
A	HOH689
A	HOH718
D	MET186
D	GLU307
D	GLU332
D	HIS447
D	HIS448
D	MN501
D	HOH623

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 503

Chain	Residue
A	GLU307
A	GLU332
A	HIS349
A	HIS448
A	SST501

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE SST B 501

Chain	Residue
B	MET186
B	GLU307
B	GLU332
B	HIS349
B	MET350
B	ILE371
B	HIS447
B	HIS448
B	MN502
B	HOH642
B	HOH783
F	GLN17
F	TYR20
F	PHE84
F	GLN126
F	HIS129
F	HOH640

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 502

Chain	Residue
B	GLU307
B	GLU332
B	HIS349
B	HIS448
B	SST501

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE SST C 501

Chain	Residue
B	TYR20
B	PHE84
B	GLN126
B	HIS129
C	MET186
C	GLU307
C	GLU332
C	MET350
C	ILE371
C	HIS447
C	HIS448
C	MN503
C	HOH620
C	HOH658

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE SST C 502

Chain	Residue
C	GLN17
C	LEU19
C	TYR20
C	PHE84
C	GLN126
C	HIS129
C	HOH746
F	MET186
F	GLU307
F	GLU332
F	HIS349
F	HIS447
F	HIS448
F	MN501
F	HOH632
F	HOH638

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 503

Chain	Residue
C	GLU307
C	GLU332
C	HIS349
C	HIS448
C	SST501

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 501

Chain	Residue
A	SST502
D	GLU307
D	GLU332
D	HIS349
D	HIS448

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE SST E 501

Chain	Residue
D	GLN17
D	LEU19
D	TYR20
D	PHE84
D	GLN126
D	HIS129
E	GLU307
E	GLU332
E	HIS349
E	MET350
E	ILE371
E	HIS447
E	HIS448
E	MN502
E	HOH649
E	HOH791

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN E 502

Chain	Residue
E	GLU307
E	GLU332
E	HIS349
E	HIS448
E	SST501

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN F 501

Chain	Residue
C	SST502
F	GLU307
F	GLU332
F	HIS349
F	HIS448

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00519","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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