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4P3M

Crystal structure of serine hydroxymethyltransferase from Psychromonas ingrahamii

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
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue SO4 A 501
ChainResidue
AILE33
AALA34
ASER35
AASN345
AARG363
AHOH694
AHOH801
BTYR65

site_idAC2
Number of Residues10
Detailsbinding site for residue SO4 A 502
ChainResidue
AGLY98
ASER99
ATHR227
AHIS229
AHOH715
AHOH752
BTYR55
BGLY262
BGLY263
ASER97

site_idAC3
Number of Residues9
Detailsbinding site for residue SO4 A 503
ChainResidue
ATYR55
AGLY263
AHOH754
BSER97
BGLY98
BSER99
BTHR227
BHIS229
BLYS230

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 504
ChainResidue
AARG81
AHOH670
AHOH783

site_idAC5
Number of Residues6
Detailsbinding site for residue CL A 505
ChainResidue
ATHR227
AHIS229
ALYS230
ATHR231
ALEU232
AHOH653

site_idAC6
Number of Residues4
Detailsbinding site for residue CL A 506
ChainResidue
AARG42
BMET6
BASN7
BHOH826

site_idAC7
Number of Residues2
Detailsbinding site for residue CL A 507
ChainResidue
AASN7
BARG42

site_idAC8
Number of Residues9
Detailsbinding site for residue GOL A 508
ChainResidue
ATYR59
AILE79
AALA91
AASN92
AASN253
AHOH644
AHOH735
AHOH753
AHOH789

site_idAC9
Number of Residues4
Detailsbinding site for residue GOL A 509
ChainResidue
APRO215
AGLN378
AHOH607
AHOH616

site_idAD1
Number of Residues7
Detailsbinding site for residue GOL A 510
ChainResidue
AALA280
AASP388
AALA405
AVAL406
ALYS409
AHOH612
AHOH615

site_idAD2
Number of Residues4
Detailsbinding site for residue GOL A 511
ChainResidue
ALYS398
ALEU399
AALA400
ATHR401

site_idAD3
Number of Residues6
Detailsbinding site for residue SO4 B 501
ChainResidue
ATYR65
BILE33
BALA34
BSER35
BARG363
BHOH689

site_idAD4
Number of Residues7
Detailsbinding site for residue GOL B 502
ChainResidue
BLEU232
BGLY233
BGLU278
BCYS279
BARG371
BHOH688
BHOH805

site_idAD5
Number of Residues4
Detailsbinding site for residue GOL B 503
ChainResidue
BVAL209
BASN216
BHOH632
BHOH726

site_idAD6
Number of Residues6
Detailsbinding site for residue GOL B 504
ChainResidue
BILE79
BALA91
BASN92
BASN253
BHOH677
BHOH681

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
ALEU121
AGLY125
ASER355
BLEU121
BGLY125
BSER355

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
AHIS229
BHIS229

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
ALYS230
BLYS230

222036

PDB entries from 2024-07-03

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