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1CJ0

CRYSTAL STRUCTURE OF RABBIT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE AT 2.8 ANGSTROM RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0000900molecular_functionmRNA regulatory element binding translation repressor activity
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006544biological_processglycine metabolic process
A0006563biological_processL-serine metabolic process
A0006565biological_processL-serine catabolic process
A0006730biological_processone-carbon metabolic process
A0009113biological_processpurine nucleobase biosynthetic process
A0016740molecular_functiontransferase activity
A0017148biological_processnegative regulation of translation
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0035999biological_processtetrahydrofolate interconversion
A0036094molecular_functionsmall molecule binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046653biological_processtetrahydrofolate metabolic process
A0046655biological_processfolic acid metabolic process
A0048027molecular_functionmRNA 5'-UTR binding
A0051289biological_processprotein homotetramerization
A0070905molecular_functionserine binding
A1904482biological_processcellular response to tetrahydrofolate
B0000900molecular_functionmRNA regulatory element binding translation repressor activity
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006544biological_processglycine metabolic process
B0006563biological_processL-serine metabolic process
B0006565biological_processL-serine catabolic process
B0006730biological_processone-carbon metabolic process
B0009113biological_processpurine nucleobase biosynthetic process
B0016740molecular_functiontransferase activity
B0017148biological_processnegative regulation of translation
B0019264biological_processglycine biosynthetic process from serine
B0030170molecular_functionpyridoxal phosphate binding
B0035999biological_processtetrahydrofolate interconversion
B0036094molecular_functionsmall molecule binding
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046653biological_processtetrahydrofolate metabolic process
B0046655biological_processfolic acid metabolic process
B0048027molecular_functionmRNA 5'-UTR binding
B0051289biological_processprotein homotetramerization
B0070905molecular_functionserine binding
B1904482biological_processcellular response to tetrahydrofolate
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP A 2291
ChainResidue
ASER97
AGLY98
ASER99
AHIS126
ASER175
AASP200
AALA202
AHIS203
ATHR226
AHIS228
ALYS229
BTYR55
BGLY262
BGLY263

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP B 2291
ChainResidue
ATYR55
AGLY262
AGLY263
BSER97
BGLY98
BSER99
BHIS126
BTHR174
BSER175
BASP200
BALA202
BHIS203
BTHR226
BHIS228
BLYS229

site_idCTA
Number of Residues6
DetailsRESIDUES COMPRISING ACTIVE SITE FOR MOLECULE A
ChainResidue
BGLU57
BTYR65
BARG363
AHIS126
ATHR226
AHIS228

site_idCTB
Number of Residues6
DetailsRESIDUES COMPRISING ACTIVE SITE FOR MOLECULE B
ChainResidue
BHIS126
BTHR226
BHIS228
AGLU57
ATYR65
AARG363

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HVvTTTTHKTLrGCRAG
ChainResidueDetails
AHIS221-GLY237

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:7358720
ChainResidueDetails
ATYR177
BTYR177

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
ALYS229
BLYS229

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10387080
ChainResidueDetails
ATHR230
BTHR230

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
AARG63

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
BARG63

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
ATHR226
ALYS229
AGLU57

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
BTHR226
BLYS229
BGLU57

site_idMCSA1
Number of Residues6
DetailsM-CSA 147
ChainResidueDetails
ASER56steric locator
AGLY58hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AMET201electrostatic stabiliser
ATHR227electrostatic stabiliser, hydrogen bond acceptor
ATHR230covalently attached, electron pair acceptor, electron pair donor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
AALA236electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 147
ChainResidueDetails
BSER56steric locator
BGLY58hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BMET201electrostatic stabiliser
BTHR227electrostatic stabiliser, hydrogen bond acceptor
BTHR230covalently attached, electron pair acceptor, electron pair donor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BALA236electrostatic stabiliser

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PDB entries from 2024-11-06

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