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3M5U

Crystal Structure of Phosphoserine Aminotransferase from Campylobacter jejuni

Functional Information from GO Data
ChainGOidnamespacecontents
A0004648molecular_functionO-phospho-L-serine:2-oxoglutarate aminotransferase activity
A0005737cellular_componentcytoplasm
A0006563biological_processL-serine metabolic process
A0006564biological_processL-serine biosynthetic process
A0008483molecular_functiontransaminase activity
A0008615biological_processpyridoxine biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0004648molecular_functionO-phospho-L-serine:2-oxoglutarate aminotransferase activity
B0005737cellular_componentcytoplasm
B0006563biological_processL-serine metabolic process
B0006564biological_processL-serine biosynthetic process
B0008483molecular_functiontransaminase activity
B0008615biological_processpyridoxine biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 361
ChainResidue
AGLN155
AASN156
ATYR157
AARG175
ALYS176
AVAL177
AASP178
AHOH447

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MES A 362
ChainResidue
AALA75
ASER76
ATRP100
ATHR148
AASP167
ASER169
AGLN190
ALYS191
AHOH531
BASN233
BTHR234
AGLY74

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MES B 361
ChainResidue
AASN233
ATHR234
BGLY74
BALA75
BSER76
BTRP100
BTHR148
BASP167
BSER169
BGLN190
BLYS191

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00160
ChainResidueDetails
AARG41
BTRP100
BTHR148
BASP167
BGLN190
BASN233
AALA75
ATRP100
ATHR148
AASP167
AGLN190
AASN233
BARG41
BALA75

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00160
ChainResidueDetails
ALYS191
BLYS191

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PDB entries from 2024-07-31

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