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6CCZ

Crystal structure of Medicago truncatula serine hydroxymethyltransferase 3 (MtSHMT3) soaked with selenourea

Functional Information from GO Data
ChainGOidnamespacecontents
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0035999biological_processtetrahydrofolate interconversion
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0019264biological_processglycine biosynthetic process from serine
B0030170molecular_functionpyridoxal phosphate binding
B0035999biological_processtetrahydrofolate interconversion
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue SEY A 601
ChainResidue
APRO183
ALEU352

site_idAC2
Number of Residues4
Detailsbinding site for residue SEY A 602
ChainResidue
AASP375
AASN378
ATYR379
AHOH738

site_idAC3
Number of Residues4
Detailsbinding site for residue SEY A 603
ChainResidue
AHOH711
AVAL174
AGLU341
ASEY606

site_idAC4
Number of Residues5
Detailsbinding site for residue SEY A 604
ChainResidue
ATYR370
ASER373
APRO374
AASP375
BSER88

site_idAC5
Number of Residues4
Detailsbinding site for residue SEY A 605
ChainResidue
AALA263
ATYR266
AARG268
AASN408

site_idAC6
Number of Residues3
Detailsbinding site for residue SEY A 606
ChainResidue
AILE155
AGLN158
ASEY603

site_idAC7
Number of Residues5
Detailsbinding site for residue SEY A 607
ChainResidue
AGLY137
AASN345
AASN346
APHE349
APRO350

site_idAC8
Number of Residues4
Detailsbinding site for residue SEY A 608
ChainResidue
AHIS196
AHOH816
BPRO195
BHOH733

site_idAC9
Number of Residues3
Detailsbinding site for residue SEY A 609
ChainResidue
APHE82
AASP84
APRO531

site_idAD1
Number of Residues2
Detailsbinding site for residue SEY A 610
ChainResidue
BLYS520
BGLN527

site_idAD2
Number of Residues4
Detailsbinding site for residue SEY A 611
ChainResidue
ALEU83
ASER119
ATYR370
AHOH723

site_idAD3
Number of Residues9
Detailsbinding site for residue ACT A 612
ChainResidue
ASER114
ATYR134
AGLU136
ATYR144
AHIS209
ASER264
AHIS292
ALLP318
AARG454

site_idAD4
Number of Residues8
Detailsbinding site for residue FMT A 613
ChainResidue
AALA291
ASER294
ATHR315
ATHR316
AHIS317
ALLP318
ASER319
ALEU320

site_idAD5
Number of Residues4
Detailsbinding site for residue SEY B 601
ChainResidue
BALA263
BTYR266
BARG268
BASN408

site_idAD6
Number of Residues2
Detailsbinding site for residue SEY B 602
ChainResidue
BLEU352
BHOH737

site_idAD7
Number of Residues4
Detailsbinding site for residue SEY B 603
ChainResidue
BILE155
BGLN158
BLEU490
BSER492

site_idAD8
Number of Residues4
Detailsbinding site for residue SEY B 604
ChainResidue
BGLN158
BVAL174
BLYS332
BGLU341

site_idAD9
Number of Residues5
Detailsbinding site for residue SEY B 605
ChainResidue
BPHE82
BASP84
BPRO529
BILE530
BPRO531

site_idAE1
Number of Residues3
Detailsbinding site for residue SEY B 606
ChainResidue
BVAL395
BLEU401
BGLY404

site_idAE2
Number of Residues5
Detailsbinding site for residue SEY B 607
ChainResidue
BLEU83
BALA90
BSER119
BTYR370
BHOH705

site_idAE3
Number of Residues6
Detailsbinding site for residue SEY B 608
ChainResidue
BGLY140
BARG142
BTYR144
BGLU426
BHOH729
BHOH789

site_idAE4
Number of Residues8
Detailsbinding site for residue ACT B 609
ChainResidue
BSER114
BTYR134
BTYR144
BHIS209
BSER264
BHIS292
BLYS318
BARG454

site_idAE5
Number of Residues5
Detailsbinding site for residue ACT B 610
ChainResidue
BSER180
BGLY181
BSER182
BGLY354
BTYR134

site_idAE6
Number of Residues9
Detailsbinding site for residue FMT B 611
ChainResidue
BALA291
BSER294
BTHR314
BTHR315
BTHR316
BHIS317
BLYS318
BSER319
BLEU320

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DIvTTTTHKSLrGPRGG
ChainResidueDetails
AASP310-GLY326
BASP310-GLY326

238268

PDB entries from 2025-07-02

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