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1RCQ

The 1.45 A crystal structure of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0006522biological_processalanine metabolic process
A0008784molecular_functionalanine racemase activity
A0016853molecular_functionisomerase activity
A0030170molecular_functionpyridoxal phosphate binding
A0030632biological_processD-alanine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP A 358
ChainResidue
AVAL31
AARG208
AGLY210
AILE211
ATYR341
ADLY359
AHOH531
AHOH603
ALYS33
ATYR37
AKCX122
AARG129
AHIS158
AASN192
ASER193
APRO194

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE DLY A 359
ChainResidue
ALYS33
ATYR37
AARG129
ATYR253
ATYR272
ASER300
AMET301
AASP302
AMET303
ATYR341
APLP358
AHOH518
AHOH601
AHOH603

Functional Information from PROSITE/UniProt
site_idPS00395
Number of Residues11
DetailsALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AViKADAYGHG
ChainResidueDetails
AALA30-GLY40

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201
ChainResidueDetails
ALYS33

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201
ChainResidueDetails
ATYR253

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:14674749
ChainResidueDetails
AARG129

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01201
ChainResidueDetails
AMET301

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:14674749
ChainResidueDetails
ALYS33

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-carboxylysine => ECO:0000269|PubMed:14674749
ChainResidueDetails
AKCX122

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
ALYS33
AARG129

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PDB entries from 2025-06-18

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