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2VMY

Crystal structure of F351GbsSHMT in complex with Gly and FTHF

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006545biological_processglycine biosynthetic process
A0006565biological_processL-serine catabolic process
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
A0008652biological_processamino acid biosynthetic process
A0016740molecular_functiontransferase activity
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0035999biological_processtetrahydrofolate interconversion
A0046653biological_processtetrahydrofolate metabolic process
A0046655biological_processfolic acid metabolic process
A0050897molecular_functioncobalt ion binding
A0070905molecular_functionserine binding
B0003824molecular_functioncatalytic activity
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006545biological_processglycine biosynthetic process
B0006565biological_processL-serine catabolic process
B0006730biological_processone-carbon metabolic process
B0008270molecular_functionzinc ion binding
B0008652biological_processamino acid biosynthetic process
B0016740molecular_functiontransferase activity
B0019264biological_processglycine biosynthetic process from serine
B0030170molecular_functionpyridoxal phosphate binding
B0035999biological_processtetrahydrofolate interconversion
B0046653biological_processtetrahydrofolate metabolic process
B0046655biological_processfolic acid metabolic process
B0050897molecular_functioncobalt ion binding
B0070905molecular_functionserine binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP A 501
ChainResidue
ASER93
ATHR223
AHIS225
ALYS226
AGLY502
BTYR51
BGLY256
BGLY257
AGLY94
AALA95
AHIS122
AALA171
ASER172
AASP197
AALA199
AHIS200

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GLY A 502
ChainResidue
ASER31
AHIS200
ALYS226
AARG357
APLP501
BTYR51
BTYR61
BFFO505

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE FFO A 505
ChainResidue
AGLU53
ATYR60
ATYR61
ALYS248
APHE251
BLEU117
BGLY120
BGLY121
BHIS122
BLEU123
BVAL129
BSER172
BASN341
BSER349
BPRO350
BGLY351
BGLY502

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLP B 501
ChainResidue
ATYR51
AGLY256
AGLY257
BSER93
BGLY94
BALA95
BHIS122
BALA171
BSER172
BASP197
BALA199
BHIS200
BTHR223
BHIS225
BLYS226
BGLY502
BHOH2003

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GLY B 502
ChainResidue
ATYR51
ATYR61
AFFO505
BSER31
BHIS200
BLYS226
BARG357
BPLP501

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE FFO B 505
ChainResidue
ALEU117
AGLY120
AGLY121
AHIS122
ALEU123
AVAL129
AASN339
AASN341
ASER349
APRO350
AGLY351
AARG357
AGLY502
BGLU53
BTYR60
BTYR61
BPHE251

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MRD B 701
ChainResidue
ATYR136
BGLN135

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HFvTTTTHKTLrGPRGG
ChainResidueDetails
AHIS218-GLY234

221051

PDB entries from 2024-06-12

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