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1XQL

Effect of a Y265F Mutant on the Transamination Based Cycloserine Inactivation of Alanine Racemase

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 Residues14
DetailsBINDING SITE FOR RESIDUE PMP A 501
ChainResidue
ALYS39
ATYR354
AHOH661
AHOH670
AHOH695
BPHE265
ATYR43
AARG136
AHIS166
AASN203
ASER204
AARG219
AGLY221
AILE222

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE PMH A 503
ChainResidue
ALYS39
ATYR43
AKCX129
AARG136
AHIS166
AASN203
ASER204
AARG219
AGLY221
AILE222
ATYR354
AHOH661
AHOH670
AHOH695
AHOH697
BPHE265
BTYR284
BCYS311
BMET312
BHOH672

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP A 504
ChainResidue
ALYS39
ATYR43
ALEU85
AHIS166
AASN203
ASER204
AARG219
AGLY221
AILE222
ATYR354
AHOH661
AHOH670
AHOH695

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 4AX B 505
ChainResidue
ALYS39
AARG136
APLP504
AHOH697
BPHE265
BTYR284
BCYS311
BMET312
BHOH672

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PMP B 601
ChainResidue
BVAL37
BLYS39
BTYR43
BARG136
BHIS166
BASN203
BSER204
BARG219
BGLY221
BILE222
BTYR354
BHOH605
BHOH643
BHOH678

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE PMH B 603
ChainResidue
APHE265
ATYR284
ACYS311
AMET312
AHOH678
BLYS39
BTYR43
BARG136
BHIS166
BASN203
BSER204
BARG219
BGLY221
BILE222
BTYR354
BHOH605
BHOH628
BHOH643
BHOH678

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP B 604
ChainResidue
BTYR354
BHOH605
BHOH678
BLYS39
BTYR43
BLEU85
BARG136
BHIS166
BASN203
BSER204
BARG219
BGLY221
BILE222

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 4AX A 605
ChainResidue
APHE265
ATYR284
AMET312
AHOH678
AHOH746
BLYS39
BARG136
BTYR354
BHOH628

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 502
ChainResidue
ALYS39
AARG136
BPHE265
BCYS311
BMET312

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 602
ChainResidue
APHE265
ACYS311
AMET312
BLYS39
BARG136

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
APHE265
BPHE265

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
APHE265
BARG136
BLYS39

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
AARG136
ALYS39
BCYS311
BPHE265

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
APHE265hydrogen 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
BPHE265hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BCYS311electrostatic stabiliser
BASP313electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2024-07-10

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