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4FUA

L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0005996biological_processmonosaccharide metabolic process
A0006004biological_processfucose metabolic process
A0008270molecular_functionzinc ion binding
A0008738molecular_functionL-fuculose-phosphate aldolase activity
A0016829molecular_functionlyase activity
A0016830molecular_functioncarbon-carbon lyase activity
A0016832molecular_functionaldehyde-lyase activity
A0019317biological_processfucose catabolic process
A0019323biological_processpentose catabolic process
A0019568biological_processarabinose catabolic process
A0019571biological_processD-arabinose catabolic process
A0042355biological_processL-fucose catabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 216
ChainResidue
AHIS92
AHIS94
ATYR113
AHIS155
APGH217

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 300
ChainResidue
AASN146
AARG147
AARG147

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 301
ChainResidue
ACYS14
AILE45
AHOH460

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PGH A 217
ChainResidue
ATHR26
AGLY28
AASN29
ATHR43
AGLY44
ASER71
ASER72
AGLU73
AHIS92
AHIS94
ATYR113
AHIS155
AZN216
AHOH431

site_idACT
Number of Residues6
DetailsTHE ACTIVE CENTER IS DEFINED BY THE ZINC ION, THE FOUR ZINC COORDINATING RESIDUES AND TYR-1 13 FROM THE ADJACENT SUBUNIT.
ChainResidue
AZN216
AGLU73
AHIS92
AHIS94
AHIS155
ATYR113

site_idPBS
Number of Residues5
DetailsBINDING SITE FOR THE SUBSTRATE PHOSPHATE GROUP.
ChainResidue
ATHR43
AGLY44
ASER71
ASER72
AASN29

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289
ChainResidueDetails
AGLU73

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:4FUA
ChainResidueDetails
AGLY28
ATHR43
ASER71

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA
ChainResidueDetails
AGLU73

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E46, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA
ChainResidueDetails
AHIS92
AHIS94
AHIS155

site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Plays a key role in the stabilization of the transition state and positioning the aldehyde component => ECO:0000269|PubMed:10821675
ChainResidueDetails
ATYR113
APHE131
ATYR209

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 72
ChainResidueDetails
AGLU73hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS92metal ligand
AHIS94metal ligand
ATYR113electrostatic stabiliser, transition state stabiliser
AHIS155metal ligand
ATYR209electrostatic stabiliser, transition state stabiliser

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PDB entries from 2024-04-24

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