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1A5S

CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUOROINDOLE PROPANOL PHOSPHATE AND L-SER BOUND AS AMINO ACRYLATE TO THE BETA SITE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processtryptophan biosynthetic process
A0003824molecular_functioncatalytic activity
A0004834molecular_functiontryptophan synthase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006568biological_processtryptophan metabolic process
A0008152biological_processmetabolic process
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0016829molecular_functionlyase activity
B0000162biological_processtryptophan biosynthetic process
B0004834molecular_functiontryptophan synthase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006568biological_processtryptophan metabolic process
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0016829molecular_functionlyase activity
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 2000
ChainResidue
BGLY232
BPHE306
BSER308
BHOH1055

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FIP A 270
ChainResidue
AILE153
ATYR175
ATHR183
AGLY184
APHE212
AGLY213
AGLY234
ASER235
AHOH1050
AHOH1129
APHE22
AASP60
ALEU100

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP B 901
ChainResidue
BALA85
BHIS86
BLYS87
BGLN114
BTHR190
BGLY232
BGLY233
BGLY234
BSER235
BASN236
BGLY303
BGLU350
BSER377
BSER902
BHOH1053
BHOH1087

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SER B 902
ChainResidue
BLYS87
BTHR110
BGLY111
BALA112
BGLY113
BGLN114
BHIS115
BGLY303
BPLP901
BHOH1051

site_idS1
Number of Residues1
DetailsSUBSTRATE ANALOG BOUND TO THE ALPHA ACTIVE SITE.
ChainResidue
AFIP270

site_idS2
Number of Residues1
DetailsREACTION INTERMEDIATE BOUND TO THE BETA ACTIVE SITE.
ChainResidue
BSER902

Functional Information from PROSITE/UniProt
site_idPS00167
Number of Residues14
DetailsTRP_SYNTHASE_ALPHA Tryptophan synthase alpha chain signature. LELGvPFSDPLADG
ChainResidueDetails
ALEU48-GLY61

site_idPS00168
Number of Residues15
DetailsTRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LlHgGAHKtNqvLgQ
ChainResidueDetails
BLEU80-GLN94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
BTHR88
AASP60

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 383
ChainResidueDetails
BTHR88electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
BTHR110
BGLY378hydrogen bond donor

218853

PDB entries from 2024-04-24

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