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1RVY

E75Q MUTANT OF RABBIT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE, COMPLEX WITH GLYCINE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000900molecular_functionmRNA regulatory element binding translation repressor activity
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006544biological_processglycine metabolic process
A0006563biological_processL-serine metabolic process
A0006565biological_processL-serine catabolic process
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
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
A0050897molecular_functioncobalt ion binding
A0051289biological_processprotein homotetramerization
A0070905molecular_functionserine binding
A1904482biological_processcellular response to tetrahydrofolate
A1990830biological_processcellular response to leukemia inhibitory factor
B0000900molecular_functionmRNA regulatory element binding translation repressor activity
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006544biological_processglycine metabolic process
B0006563biological_processL-serine metabolic process
B0006565biological_processL-serine catabolic process
B0006730biological_processone-carbon metabolic process
B0008270molecular_functionzinc ion binding
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
B0050897molecular_functioncobalt ion binding
B0051289biological_processprotein homotetramerization
B0070905molecular_functionserine binding
B1904482biological_processcellular response to tetrahydrofolate
B1990830biological_processcellular response to leukemia inhibitory factor
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 B 601
ChainResidue
ATYR73
AGLN75
ATYR83
BSER53
BSER203
BHIS231
BLYS257
BARG402
BPLP600

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE PLG A 500
ChainResidue
ASER53
ASER119
AGLY120
ASER121
AASN124
AHIS148
ASER203
AASP228
AALA230
AHIS231
ATHR254
AHIS256
ALYS257
AARG402
AHOH515
BTYR73
BGLN75
BTYR83
BGLY302
BGLY303

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP B 600
ChainResidue
ATYR73
AGLY302
AGLY303
BSER119
BGLY120
BSER121
BHIS148
BASP228
BALA230
BHIS231
BTHR254
BHIS256
BLYS257
BPO4601
BHOH615

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HVvTTTTHKTLrGCRAG
ChainResidueDetails
AHIS249-GLY265

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:7358720
ChainResidueDetails
ATYR205
BTYR205

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
ALYS257
BLYS257

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:3553178
ChainResidueDetails
ATHR3
BTHR3

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Deamidated asparagine; alternate => ECO:0000269|PubMed:2318867
ChainResidueDetails
AGLY7
BGLY7

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10387080
ChainResidueDetails
ATHR258
BTHR258

site_idSWS_FT_FI6
Number of Residues4
DetailsCROSSLNK: Isoaspartyl glycine isopeptide (Asn-Gly); alternate => ECO:0000269|PubMed:2318867
ChainResidueDetails
AGLY7
AALA8
BGLY7
BALA8

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
AARG81

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
BARG81

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
AGLN75
ATHR254
ALYS257

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
BGLN75
BTHR254
BLYS257

site_idMCSA1
Number of Residues6
DetailsM-CSA 147
ChainResidueDetails
ASER74steric locator
AGLY76hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AMET229electrostatic stabiliser
ATHR255electrostatic stabiliser, hydrogen bond acceptor
ATHR258covalently attached, electron pair acceptor, electron pair donor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
AALA264electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 147
ChainResidueDetails
BSER74steric locator
BGLY76hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BMET229electrostatic stabiliser
BTHR255electrostatic stabiliser, hydrogen bond acceptor
BTHR258covalently attached, electron pair acceptor, electron pair donor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BALA264electrostatic stabiliser

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PDB entries from 2024-08-07

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