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4R1Q

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005996biological_processmonosaccharide metabolic process
A0008733molecular_functionL-arabinose isomerase activity
A0016853molecular_functionisomerase activity
A0016861molecular_functionintramolecular oxidoreductase activity, interconverting aldoses and ketoses
A0019568biological_processarabinose catabolic process
A0019569biological_processL-arabinose catabolic process to xylulose 5-phosphate
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005996biological_processmonosaccharide metabolic process
B0008733molecular_functionL-arabinose isomerase activity
B0016853molecular_functionisomerase activity
B0016861molecular_functionintramolecular oxidoreductase activity, interconverting aldoses and ketoses
B0019568biological_processarabinose catabolic process
B0019569biological_processL-arabinose catabolic process to xylulose 5-phosphate
B0030145molecular_functionmanganese ion binding
B0046872molecular_functionmetal ion binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005996biological_processmonosaccharide metabolic process
C0008733molecular_functionL-arabinose isomerase activity
C0016853molecular_functionisomerase activity
C0016861molecular_functionintramolecular oxidoreductase activity, interconverting aldoses and ketoses
C0019568biological_processarabinose catabolic process
C0019569biological_processL-arabinose catabolic process to xylulose 5-phosphate
C0030145molecular_functionmanganese ion binding
C0046872molecular_functionmetal ion binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005996biological_processmonosaccharide metabolic process
D0008733molecular_functionL-arabinose isomerase activity
D0016853molecular_functionisomerase activity
D0016861molecular_functionintramolecular oxidoreductase activity, interconverting aldoses and ketoses
D0019568biological_processarabinose catabolic process
D0019569biological_processL-arabinose catabolic process to xylulose 5-phosphate
D0030145molecular_functionmanganese ion binding
D0046872molecular_functionmetal ion binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005996biological_processmonosaccharide metabolic process
E0008733molecular_functionL-arabinose isomerase activity
E0016853molecular_functionisomerase activity
E0016861molecular_functionintramolecular oxidoreductase activity, interconverting aldoses and ketoses
E0019568biological_processarabinose catabolic process
E0019569biological_processL-arabinose catabolic process to xylulose 5-phosphate
E0030145molecular_functionmanganese ion binding
E0046872molecular_functionmetal ion binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0005996biological_processmonosaccharide metabolic process
F0008733molecular_functionL-arabinose isomerase activity
F0016853molecular_functionisomerase activity
F0016861molecular_functionintramolecular oxidoreductase activity, interconverting aldoses and ketoses
F0019568biological_processarabinose catabolic process
F0019569biological_processL-arabinose catabolic process to xylulose 5-phosphate
F0030145molecular_functionmanganese ion binding
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SST A 501
ChainResidue
AMET186
AHOH631
EGLN17
ELEU19
ETYR20
EPHE84
EGLN126
EHIS129
EHOH624
AGLU307
AGLU332
AHIS349
AMET350
AILE371
AHIS447
AHIS448
AMN503

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE SST A 502
ChainResidue
AGLN17
ALEU19
ATYR20
APHE84
AGLN126
AHIS129
AHOH689
AHOH718
DMET186
DGLU307
DGLU332
DHIS447
DHIS448
DMN501
DHOH623

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 503
ChainResidue
AGLU307
AGLU332
AHIS349
AHIS448
ASST501

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SST B 501
ChainResidue
BMET186
BGLU307
BGLU332
BHIS349
BMET350
BILE371
BHIS447
BHIS448
BMN502
BHOH642
BHOH783
FGLN17
FTYR20
FPHE84
FGLN126
FHIS129
FHOH640

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 502
ChainResidue
BGLU307
BGLU332
BHIS349
BHIS448
BSST501

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SST C 501
ChainResidue
BTYR20
BPHE84
BGLN126
BHIS129
CMET186
CGLU307
CGLU332
CMET350
CILE371
CHIS447
CHIS448
CMN503
CHOH620
CHOH658

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE SST C 502
ChainResidue
CGLN17
CLEU19
CTYR20
CPHE84
CGLN126
CHIS129
CHOH746
FMET186
FGLU307
FGLU332
FHIS349
FHIS447
FHIS448
FMN501
FHOH632
FHOH638

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN C 503
ChainResidue
CGLU307
CGLU332
CHIS349
CHIS448
CSST501

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN D 501
ChainResidue
ASST502
DGLU307
DGLU332
DHIS349
DHIS448

site_idBC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE SST E 501
ChainResidue
DGLN17
DLEU19
DTYR20
DPHE84
DGLN126
DHIS129
EGLU307
EGLU332
EHIS349
EMET350
EILE371
EHIS447
EHIS448
EMN502
EHOH649
EHOH791

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN E 502
ChainResidue
EGLU307
EGLU332
EHIS349
EHIS448
ESST501

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN F 501
ChainResidue
CSST502
FGLU307
FGLU332
FHIS349
FHIS448

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00519
ChainResidueDetails
AGLU307
CGLU332
CHIS349
CHIS448
DGLU307
DGLU332
DHIS349
DHIS448
EGLU307
EGLU332
EHIS349
AGLU332
EHIS448
FGLU307
FGLU332
FHIS349
FHIS448
AHIS349
AHIS448
BGLU307
BGLU332
BHIS349
BHIS448
CGLU307

222624

PDB entries from 2024-07-17

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