Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4F2D

Crystal Structure of Escherichia coli L-arabinose Isomerase (ECAI) complexed with Ribitol

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 601
ChainResidue
AGLU306
AGLU333
AHIS350
AHIS450
ARB0602

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE RB0 A 602
ChainResidue
ATYR335
AHIS449
AHIS450
AMN601
AHOH788
BGLN16
BLEU18
BTYR19
BPHE83
BGLN125
BHIS128
AMSE185
APHE279
AGLU306
AGLU333

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 601
ChainResidue
BGLU306
BGLU333
BHIS350
BHIS450
BRB0602

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE RB0 B 602
ChainResidue
BMSE185
BPHE279
BGLU306
BGLU333
BHIS449
BHIS450
BMN601
BHOH776
CGLN16
CTYR19
CPHE83
CGLN125
CHIS128

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY B 603
ChainResidue
ATRP491
AVAL494
BTRP491
BVAL494
CTRP491
CVAL494

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN C 601
ChainResidue
CGLU306
CGLU333
CHIS350
CHIS450
CRB0602

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE RB0 C 602
ChainResidue
AGLN125
AHIS128
CMSE185
CPHE279
CGLU306
CGLU333
CHIS449
CHIS450
CMN601

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AGLU306
CGLU333
CHIS350
CHIS450
AGLU333
AHIS350
AHIS450
BGLU306
BGLU333
BHIS350
BHIS450
CGLU306

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon