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3IJQ

Structure of dipeptide epimerase from Bacteroides thetaiotaomicron complexed with L-Ala-D-Glu; productive substrate binding.

Functional Information from GO Data
ChainGOidnamespacecontents
A0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
B0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ALA A 384
ChainResidue
APHE61
ALYS198
AASP348
AASP350
ALEU354
ADGL385
AHOH439

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE DGL A 385
ChainResidue
APRO92
ATYR94
ALYS298
ACYS326
AMET327
ATHR328
AALA384
AMG386
APHE61
AARG68

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 386
ChainResidue
AASP224
AGLU251
AASP276
ADGL385
AHOH387

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ALA B 384
ChainResidue
BLYS198
BLYS200
BCYS326
BASP348
BASP350
BDGL385

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE DGL B 385
ChainResidue
BPHE61
BVAL63
BARG68
BPRO92
BTYR94
BLYS198
BASP224
BASN226
BASP276
BLYS298
BCYS326
BMET327
BTHR328
BALA384
BMG386
BHOH388
BHOH405
BHOH432

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 386
ChainResidue
BASP224
BGLU251
BASP276
BLYS298
BDGL385
BHOH388

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 387
ChainResidue
AARG68
ATHR69
ATHR70
BLYS243
BPRO270
BHOH491

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AARG68
BLYS298
BCYS326
BASP348
ATYR94
ALYS198
ALYS298
ACYS326
AASP348
BARG68
BTYR94
BLYS198

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22392983
ChainResidueDetails
AASP224
AGLU251
AASP276
BASP224
BGLU251
BASP276

220113

PDB entries from 2024-05-22

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