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4FS9

Complex structure of a broad specificity amino acid racemase (Bar) within the reactive intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006522biological_processalanine metabolic process
A0008784molecular_functionalanine racemase activity
A0016853molecular_functionisomerase activity
B0003824molecular_functioncatalytic activity
B0006522biological_processalanine metabolic process
B0008784molecular_functionalanine racemase activity
B0016853molecular_functionisomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PE1 A 501
ChainResidue
ALYS75
AGLY264
AHOH627
AHOH639
BTYR301
BTYR320
BSER348
BMET349
ATYR79
AVAL121
AARG174
AHIS205
AASN245
ASER246
AARG261
AGLY263

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PE1 B 501
ChainResidue
ATYR301
ATYR320
ASER348
AMET349
AHOH624
BLYS75
BTYR79
BARG174
BHIS205
BASN245
BSER246
BARG261
BTHR262
BGLY263
BGLY264

Functional Information from PROSITE/UniProt
site_idPS00395
Number of Residues11
DetailsALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVlKADAYGHG
ChainResidueDetails
AALA72-GLY82

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000305|PubMed:23118975
ChainResidueDetails
ALYS75
ATYR301
BLYS75
BTYR301

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02212
ChainResidueDetails
AARG174
AMET349
BARG174
BMET349

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:23118975
ChainResidueDetails
ALYS75
BLYS75

226707

PDB entries from 2024-10-30

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