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3QM2

2.25 Angstrom Crystal Structure of Phosphoserine Aminotransferase (SerC) from Salmonella enterica subsp. enterica serovar Typhimurium

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 Residues5
DetailsBINDING SITE FOR RESIDUE CA A 363
ChainResidue
AILE280
ASER283
ATYR286
AHOH467
AHOH468

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 363
ChainResidue
BHOH459
BILE280
BSER283
BTYR286
BHOH458

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues20
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. YGVIyaGAQKnigpa.GlTlV
ChainResidueDetails
ATYR189-VAL208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00160
ChainResidueDetails
ASER9
BARG42
BGLY76
BTRP102
BTHR153
BASP174
BGLN197
BASN239
AARG42
AGLY76
ATRP102
ATHR153
AASP174
AGLN197
AASN239
BSER9

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00160
ChainResidueDetails
ALYS198
BLYS198

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PDB entries from 2024-10-09

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