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1L6F

Alanine racemase bound with N-(5'-phosphopyridoxyl)-L-alanine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0006522biological_processalanine metabolic process
A0008784molecular_functionalanine racemase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016853molecular_functionisomerase activity
A0030170molecular_functionpyridoxal phosphate binding
A0030632biological_processD-alanine biosynthetic process
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0006522biological_processalanine metabolic process
B0008784molecular_functionalanine racemase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016853molecular_functionisomerase activity
B0030170molecular_functionpyridoxal phosphate binding
B0030632biological_processD-alanine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PP3 A 390
ChainResidue
ALYS39
AHOH409
AHOH452
AHOH460
AHOH461
BTYR265
BTYR284
BCYS311
BMET312
ATYR43
AARG136
AHIS166
ASER204
AARG219
AGLY221
AILE222
ATYR354

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE PP3 B 1390
ChainResidue
ATYR265
ATYR284
ACYS311
AMET312
BLYS39
BTYR43
BKCX129
BARG136
BHIS166
BASN203
BSER204
BARG219
BGLY221
BILE222
BTYR354
BHOH459
BHOH500
BHOH504
BHOH556
BHOH565

Functional Information from PROSITE/UniProt
site_idPS00395
Number of Residues11
DetailsALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVvKANAYGHG
ChainResidueDetails
AALA36-GLY46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor; specific for D-alanine => ECO:0000305|PubMed:10502689, ECO:0000305|PubMed:15807525
ChainResidueDetails
ALYS39
BLYS39

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor; specific for L-alanine => ECO:0000305|PubMed:10502689, ECO:0000305|PubMed:15807525
ChainResidueDetails
ATYR265
BTYR265

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11886871
ChainResidueDetails
AARG136
AMET312
BARG136
BMET312

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11886871, ECO:0000269|PubMed:15807525, ECO:0000269|PubMed:9063881
ChainResidueDetails
ALYS39
BLYS39

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000269|PubMed:10079072, ECO:0000269|PubMed:11886871, ECO:0000269|PubMed:12741835, ECO:0000269|PubMed:15807525, ECO:0000269|Ref.10
ChainResidueDetails
AKCX129
BKCX129

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
ACYS311
ATYR265
BARG136
BLYS39

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
AARG136
ALYS39
BCYS311
BTYR265

site_idMCSA1
Number of Residues7
DetailsM-CSA 213
ChainResidueDetails
ALYS39covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
AARG136electrostatic stabiliser
AHIS166electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AARG219electrostatic stabiliser, hydrogen bond donor
ATYR265hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ACYS311electrostatic stabiliser
AASP313electrostatic stabiliser, hydrogen bond acceptor

site_idMCSA2
Number of Residues7
DetailsM-CSA 213
ChainResidueDetails
BLYS39covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BARG136electrostatic stabiliser
BHIS166electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BARG219electrostatic stabiliser, hydrogen bond donor
BTYR265hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BCYS311electrostatic stabiliser
BASP313electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2024-05-01

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