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4O6Z

Crystal structure of serine hydroxymethyltransferase with covalently bound PLP Schiff-base from Plasmodium falciparum

Functional Information from GO Data
ChainGOidnamespacecontents
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006730biological_processone-carbon metabolic process
A0008168molecular_functionmethyltransferase activity
A0019264biological_processglycine biosynthetic process from serine
A0020011cellular_componentapicoplast
A0030170molecular_functionpyridoxal phosphate binding
A0032259biological_processmethylation
A0035999biological_processtetrahydrofolate interconversion
A0042803molecular_functionprotein homodimerization activity
A0046653biological_processtetrahydrofolate metabolic process
A0070178biological_processD-serine metabolic process
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006730biological_processone-carbon metabolic process
B0008168molecular_functionmethyltransferase activity
B0019264biological_processglycine biosynthetic process from serine
B0020011cellular_componentapicoplast
B0030170molecular_functionpyridoxal phosphate binding
B0032259biological_processmethylation
B0035999biological_processtetrahydrofolate interconversion
B0042803molecular_functionprotein homodimerization activity
B0046653biological_processtetrahydrofolate metabolic process
B0070178biological_processD-serine metabolic process
C0004372molecular_functionglycine hydroxymethyltransferase activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0006730biological_processone-carbon metabolic process
C0008168molecular_functionmethyltransferase activity
C0019264biological_processglycine biosynthetic process from serine
C0020011cellular_componentapicoplast
C0030170molecular_functionpyridoxal phosphate binding
C0032259biological_processmethylation
C0035999biological_processtetrahydrofolate interconversion
C0042803molecular_functionprotein homodimerization activity
C0046653biological_processtetrahydrofolate metabolic process
C0070178biological_processD-serine metabolic process
D0004372molecular_functionglycine hydroxymethyltransferase activity
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0006730biological_processone-carbon metabolic process
D0008168molecular_functionmethyltransferase activity
D0019264biological_processglycine biosynthetic process from serine
D0020011cellular_componentapicoplast
D0030170molecular_functionpyridoxal phosphate binding
D0032259biological_processmethylation
D0035999biological_processtetrahydrofolate interconversion
D0042803molecular_functionprotein homodimerization activity
D0046653biological_processtetrahydrofolate metabolic process
D0070178biological_processD-serine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP A 701
ChainResidue
ASER100
ALYS237
AHOH832
BTYR54
BGLY272
AGLY101
ASER102
AHIS129
AASP208
ASER210
AHIS211
ATHR234
AHIS236

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP B 701
ChainResidue
ATYR54
AGLY272
BSER100
BGLY101
BSER102
BHIS129
BTHR183
BASP208
BSER210
BHIS211
BTHR234
BHIS236
BLYS237
BHOH832

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP C 701
ChainResidue
CSER100
CGLY101
CSER102
CHIS129
CTHR183
CASP208
CSER210
CHIS211
CTHR234
CHIS236
CLYS237
DTYR54
DGLY271
DGLY272

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 D 501
ChainResidue
CTYR54
CGLY271
CGLY272
DSER100
DGLY101
DSER102
DTHR234

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:24914963, ECO:0007744|PDB:4O6Z
ChainResidueDetails
ATYR54
AGLY272
BTYR54
BGLY272
CTYR54
CGLY272
DTYR54
DGLY272

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: in other chain => ECO:0000269|PubMed:24914963, ECO:0007744|PDB:4O6Z
ChainResidueDetails
ASER100
AHIS236
BSER100
BHIS236
CSER100
CHIS236
DSER100
DHIS236

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|PIRSR:PIRSR000412-50, ECO:0000269|PubMed:24914963, ECO:0007744|PDB:4O6Z
ChainResidueDetails
ALYS237
BLYS237
CLYS237
DLYS237

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PDB entries from 2024-10-30

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