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7CJ6

Crystal structure of homo dimeric D-allulose 3-epimerase from Methylomonas sp. in complex with D-allulose

Functional Information from GO Data
ChainGOidnamespacecontents
A0016853molecular_functionisomerase activity
A0046872molecular_functionmetal ion binding
B0016853molecular_functionisomerase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MN A 301
ChainResidue
AGLU152
AASP185
AHIS211
AGLU246
APSJ302

site_idAC2
Number of Residues14
Detailsbinding site for residue PSJ A 302
ChainResidue
ALEU116
AGLU152
AGLU158
AASP185
AHIS188
AHIS211
AARG217
AGLU246
ALEU261
AMN301
AHIS12
AGLU41
AALA43
ASER69

site_idAC3
Number of Residues5
Detailsbinding site for residue MN B 301
ChainResidue
BGLU152
BASP185
BHIS211
BGLU246
BPSJ302

site_idAC4
Number of Residues14
Detailsbinding site for residue PSJ B 302
ChainResidue
BHIS12
BSER69
BGLY110
BVAL111
BLEU116
BGLU152
BGLU158
BASP185
BHIS188
BHIS211
BARG217
BGLU246
BLEU261
BMN301

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GMAKsvLAaGDRLG
ChainResidueDetails
AGLY195-GLY208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q9WYP7
ChainResidueDetails
AGLU152
AGLU246
BGLU152
BGLU246

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:33838083, ECO:0007744|PDB:7CJ5, ECO:0007744|PDB:7CJ9
ChainResidueDetails
AHIS12
BARG217
ASER69
AGLU158
AHIS188
AARG217
BHIS12
BSER69
BGLU158
BHIS188

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:33838083, ECO:0000312|PDB:7CJ5, ECO:0007744|PDB:7CJ4, ECO:0007744|PDB:7CJ6, ECO:0007744|PDB:7CJ7, ECO:0007744|PDB:7CJ8, ECO:0007744|PDB:7CJ9
ChainResidueDetails
AGLU152
AASP185
AHIS211
AGLU246
BGLU152
BASP185
BHIS211
BGLU246

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PDB entries from 2024-07-17

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