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6YMD

Crystal structure of serine hydroxymethyltransferase from Aphanothece halophytica in the covalent complex with malonate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006544biological_processglycine metabolic process
A0006545biological_processglycine biosynthetic process
A0006563biological_processL-serine metabolic process
A0006730biological_processone-carbon metabolic process
A0008168molecular_functionmethyltransferase activity
A0008652biological_processamino acid biosynthetic process
A0016740molecular_functiontransferase activity
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0032259biological_processmethylation
A0035999biological_processtetrahydrofolate interconversion
A0046653biological_processtetrahydrofolate metabolic process
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006544biological_processglycine metabolic process
B0006545biological_processglycine biosynthetic process
B0006563biological_processL-serine metabolic process
B0006730biological_processone-carbon metabolic process
B0008168molecular_functionmethyltransferase activity
B0008652biological_processamino acid biosynthetic process
B0016740molecular_functiontransferase activity
B0019264biological_processglycine biosynthetic process from serine
B0030170molecular_functionpyridoxal phosphate binding
B0032259biological_processmethylation
B0035999biological_processtetrahydrofolate interconversion
B0046653biological_processtetrahydrofolate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue EDO A 502
ChainResidue
APRO42
ATYR416
AHOH818
AHOH873

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 503
ChainResidue
APRO133
AHIS145
AGLN332
AHOH982

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 505
ChainResidue
ALEU323
AVAL326
ALEU328
AHOH800
AHOH831
AGLU142

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO B 503
ChainResidue
BGLN21
BGLN25
BHOH635
BHOH728

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO B 504
ChainResidue
BLYS170
BGLY196
BHOH676
BHOH740

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO B 505
ChainResidue
BLEU86
BVAL210
BALA211
BGLN404
BHOH601
BHOH602

site_idAC7
Number of Residues6
Detailsbinding site for residue NA B 506
ChainResidue
BGLY138
BPHE141
BHOH830
BHOH857
BHOH878
BHOH969

site_idAC8
Number of Residues22
Detailsbinding site for residues PMP A 501 and MLI B 501
ChainResidue
ASER36
ASER98
AGLY99
AALA100
AHIS127
ASER177
AASP202
AALA204
AHIS205
ATHR228
AHIS230
ALYS231
AARG363
AHOH655
AHOH664
AHOH811
BTYR56
BGLU58
BTYR66
BGLY262
BGLY263
BHOH646

site_idAC9
Number of Residues30
Detailsbinding site for residues MLI A 504 and PMP B 502
ChainResidue
APRO42
ATYR56
AGLU58
ATYR66
AGLY262
AGLY263
ATYR416
AHOH614
AHOH818
AHOH873
BSER36
BSER98
BGLY99
BALA100
BHIS127
BLYS170
BSER177
BGLY196
BASP202
BALA204
BHIS205
BTHR228
BHIS230
BLYS231
BARG363
BHOH655
BHOH676
BHOH737
BHOH740
BHOH820

site_idAD1
Number of Residues24
Detailsbinding site for Di-peptide PMP B 502 and LYS B 231
ChainResidue
BHIS205
BTHR228
BHIS230
BTHR232
BLEU233
BARG234
BHOH655
BHOH699
BHOH737
BHOH820
BHOH835
ATYR56
AGLY262
AGLY263
AMLI504
BSER36
BASN38
BSER98
BGLY99
BALA100
BHIS127
BSER177
BASP202
BALA204

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DVvTTTTHKTLrGPRGG
ChainResidueDetails
AASP223-GLY239

239492

PDB entries from 2025-07-30

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