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6L0Q

Crystal Structure of the O-Phosphoserine Sulfhydrylase from Aeropyrum pernix Complexed with O-Phosphoserine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004122molecular_functioncystathionine beta-synthase activity
A0004124molecular_functioncysteine synthase activity
A0005737cellular_componentcytoplasm
A0006534biological_processcysteine metabolic process
A0006535biological_processcysteine biosynthetic process from serine
A0009069biological_processserine family amino acid metabolic process
A0016740molecular_functiontransferase activity
A0016829molecular_functionlyase activity
A0019344biological_processcysteine biosynthetic process
A0033847molecular_functionO-phosphoserine sulfhydrylase activity
A0044272biological_processsulfur compound biosynthetic process
B0004122molecular_functioncystathionine beta-synthase activity
B0004124molecular_functioncysteine synthase activity
B0005737cellular_componentcytoplasm
B0006534biological_processcysteine metabolic process
B0006535biological_processcysteine biosynthetic process from serine
B0009069biological_processserine family amino acid metabolic process
B0016740molecular_functiontransferase activity
B0016829molecular_functionlyase activity
B0019344biological_processcysteine biosynthetic process
B0033847molecular_functionO-phosphoserine sulfhydrylase activity
B0044272biological_processsulfur compound biosynthetic process
C0004122molecular_functioncystathionine beta-synthase activity
C0004124molecular_functioncysteine synthase activity
C0005737cellular_componentcytoplasm
C0006534biological_processcysteine metabolic process
C0006535biological_processcysteine biosynthetic process from serine
C0009069biological_processserine family amino acid metabolic process
C0016740molecular_functiontransferase activity
C0016829molecular_functionlyase activity
C0019344biological_processcysteine biosynthetic process
C0033847molecular_functionO-phosphoserine sulfhydrylase activity
C0044272biological_processsulfur compound biosynthetic process
D0004122molecular_functioncystathionine beta-synthase activity
D0004124molecular_functioncysteine synthase activity
D0005737cellular_componentcytoplasm
D0006534biological_processcysteine metabolic process
D0006535biological_processcysteine biosynthetic process from serine
D0009069biological_processserine family amino acid metabolic process
D0016740molecular_functiontransferase activity
D0016829molecular_functionlyase activity
D0019344biological_processcysteine biosynthetic process
D0033847molecular_functionO-phosphoserine sulfhydrylase activity
D0044272biological_processsulfur compound biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue E1U A 401
ChainResidue
ATHR152
ATHR262
ASER263
AGLY264
AHIS265
AGLY295
AILE296
AARG297
ASER341
APRO368
ATYR374
ASER153
AHOH503
AHOH509
AHOH525
AHOH545
AASN155
APHE156
ATHR203
AGLN224
ATYR225
ASER259
AGLY261

site_idAC2
Number of Residues22
Detailsbinding site for residue E1U B 401
ChainResidue
BTHR152
BSER153
BASN155
BPHE156
BTHR203
BGLN224
BTYR225
BSER259
BGLY261
BTHR262
BSER263
BGLY264
BHIS265
BGLY295
BILE296
BARG297
BSER341
BPRO368
BHOH510
BHOH522
BHOH527
BHOH551

site_idAC3
Number of Residues11
Detailsbinding site for residue MPD B 402
ChainResidue
AMET82
APHE90
AGLY94
APRO96
ATHR97
ATYR119
AHOH508
BMET82
BGLY94
BTYR119
BHOH503

site_idAC4
Number of Residues24
Detailsbinding site for residue E1U C 401
ChainResidue
CTHR152
CSER153
CASN155
CPHE156
CTHR203
CGLN224
CTYR225
CSER259
CGLY261
CTHR262
CSER263
CGLY264
CHIS265
CGLY295
CILE296
CARG297
CSER341
CPRO368
CASP369
CTYR374
CHOH505
CHOH507
CHOH519
CHOH531

site_idAC5
Number of Residues10
Detailsbinding site for residue MPD C 402
ChainResidue
CMET82
CPHE90
CGLY94
CPRO96
CTHR97
CTYR119
CHOH502
CHOH516
DMET82
DTYR119

site_idAC6
Number of Residues24
Detailsbinding site for residue E1U D 401
ChainResidue
DGLY261
DTHR262
DSER263
DGLY264
DHIS265
DGLY295
DILE296
DARG297
DSER341
DPRO368
DTYR374
DHOH505
DHOH506
DHOH507
DHOH549
DTHR152
DSER153
DASN155
DPHE156
DTHR203
DGLN224
DTYR225
DSER259
DLEU260

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16005886
ChainResidueDetails
AASN155
ASER341
BASN155
BSER341
CASN155
CSER341
DASN155
DSER341

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AGLY261
BGLY261
CGLY261
DGLY261

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
AALA127
BALA127
CALA127
DALA127

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PDB entries from 2024-10-30

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