Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4OT8

X-ray Crystal Structure of Serine Hydroxymethyl Transferase from Burkholderia cenocepacia bound to PLP and Serine

Functional Information from GO Data
ChainGOidnamespacecontents
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
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
C0004372molecular_functionglycine hydroxymethyltransferase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006545biological_processglycine biosynthetic process
C0006565biological_processL-serine catabolic process
C0006730biological_processone-carbon metabolic process
C0008270molecular_functionzinc ion binding
C0008652biological_processamino acid biosynthetic process
C0016740molecular_functiontransferase activity
C0019264biological_processglycine biosynthetic process from serine
C0030170molecular_functionpyridoxal phosphate binding
C0035999biological_processtetrahydrofolate interconversion
C0046653biological_processtetrahydrofolate metabolic process
C0046655biological_processfolic acid metabolic process
C0050897molecular_functioncobalt ion binding
C0070905molecular_functionserine binding
D0004372molecular_functionglycine hydroxymethyltransferase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006545biological_processglycine biosynthetic process
D0006565biological_processL-serine catabolic process
D0006730biological_processone-carbon metabolic process
D0008270molecular_functionzinc ion binding
D0008652biological_processamino acid biosynthetic process
D0016740molecular_functiontransferase activity
D0019264biological_processglycine biosynthetic process from serine
D0030170molecular_functionpyridoxal phosphate binding
D0035999biological_processtetrahydrofolate interconversion
D0046653biological_processtetrahydrofolate metabolic process
D0046655biological_processfolic acid metabolic process
D0050897molecular_functioncobalt ion binding
D0070905molecular_functionserine binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP A 501
ChainResidue
ASER98
ALYS230
ASER502
AHOH763
CTYR56
CGLY260
CGLY261
CHOH804
AGLY99
ASER100
AHIS127
ASER176
AASP201
AHIS204
ATHR227
AHIS229

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SER A 502
ChainResidue
ASER36
AHIS127
AHIS204
ALYS230
AARG361
APLP501
CTYR56
CGLU58
CTYR66

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SER A 503
ChainResidue
ATYR56
AGLU58
ATYR66
CSER36
CHIS127
CHIS204
CLYS230
CARG361
CPLP700

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PLP B 501
ChainResidue
BSER98
BGLY99
BSER100
BHIS127
BSER176
BASP201
BALA203
BHIS204
BTHR227
BHIS229
BLYS230
BSER502
BHOH760
DTYR56
DGLY260
DGLY261
DHOH938
DHOH1004

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SER B 502
ChainResidue
BSER36
BHIS127
BSER176
BHIS204
BLYS230
BARG361
BPLP501
DGLU58
DTYR66

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SER B 503
ChainResidue
BTYR56
BGLU58
BTYR66
DSER36
DHIS127
DHIS204
DARG361
DPLP800

site_idAC7
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PLP C 700
ChainResidue
ATYR56
AGLY260
AGLY261
ASER503
AHOH642
CSER98
CGLY99
CSER100
CHIS127
CALA175
CSER176
CASP201
CALA203
CHIS204
CTHR227
CHIS229
CLYS230
CHOH894

site_idAC8
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLP D 800
ChainResidue
DHIS204
DTHR227
DHIS229
DLYS230
DHOH1002
BTYR56
BGLY260
BGLY261
BSER503
BHOH672
DSER98
DGLY99
DSER100
DHIS127
DALA175
DSER176
DASP201

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DFvTTTTHKSLrGPRGG
ChainResidueDetails
AASP222-GLY238

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon