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5TXT

Structure of asymmetric apo/holo ALAS dimer from S. cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0003870molecular_function5-aminolevulinate synthase activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0006783biological_processheme biosynthetic process
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0033014biological_processtetrapyrrole biosynthetic process
A1902117biological_processpositive regulation of organelle assembly
B0003870molecular_function5-aminolevulinate synthase activity
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006782biological_processprotoporphyrinogen IX biosynthetic process
B0006783biological_processheme biosynthetic process
B0009058biological_processbiosynthetic process
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0030170molecular_functionpyridoxal phosphate binding
B0033014biological_processtetrapyrrole biosynthetic process
B1902117biological_processpositive regulation of organelle assembly
C0003870molecular_function5-aminolevulinate synthase activity
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0006782biological_processprotoporphyrinogen IX biosynthetic process
C0006783biological_processheme biosynthetic process
C0009058biological_processbiosynthetic process
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0030170molecular_functionpyridoxal phosphate binding
C0033014biological_processtetrapyrrole biosynthetic process
C1902117biological_processpositive regulation of organelle assembly
D0003870molecular_function5-aminolevulinate synthase activity
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0006782biological_processprotoporphyrinogen IX biosynthetic process
D0006783biological_processheme biosynthetic process
D0009058biological_processbiosynthetic process
D0016740molecular_functiontransferase activity
D0016746molecular_functionacyltransferase activity
D0030170molecular_functionpyridoxal phosphate binding
D0033014biological_processtetrapyrrole biosynthetic process
D1902117biological_processpositive regulation of organelle assembly
E0003870molecular_function5-aminolevulinate synthase activity
E0005739cellular_componentmitochondrion
E0005759cellular_componentmitochondrial matrix
E0006782biological_processprotoporphyrinogen IX biosynthetic process
E0006783biological_processheme biosynthetic process
E0009058biological_processbiosynthetic process
E0016740molecular_functiontransferase activity
E0016746molecular_functionacyltransferase activity
E0030170molecular_functionpyridoxal phosphate binding
E0033014biological_processtetrapyrrole biosynthetic process
E1902117biological_processpositive regulation of organelle assembly
F0003870molecular_function5-aminolevulinate synthase activity
F0005739cellular_componentmitochondrion
F0005759cellular_componentmitochondrial matrix
F0006782biological_processprotoporphyrinogen IX biosynthetic process
F0006783biological_processheme biosynthetic process
F0009058biological_processbiosynthetic process
F0016740molecular_functiontransferase activity
F0016746molecular_functionacyltransferase activity
F0030170molecular_functionpyridoxal phosphate binding
F0033014biological_processtetrapyrrole biosynthetic process
F1902117biological_processpositive regulation of organelle assembly
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue PE3 B 601
ChainResidue
BASN439
BLYS440
BPE3602
BPE3603
BHOH716

site_idAC2
Number of Residues4
Detailsbinding site for residue PE3 B 602
ChainResidue
BALA311
BTHR312
BPE3601
BPE3603

site_idAC3
Number of Residues3
Detailsbinding site for residue PE3 B 603
ChainResidue
BPE3601
BPE3602
BHOH742

site_idAC4
Number of Residues2
Detailsbinding site for residue SO4 D 601
ChainResidue
DSER256
DHIS284

site_idAC5
Number of Residues6
Detailsbinding site for residue PE3 C 601
ChainResidue
CTHR312
CPE3602
CPE3603
CHOH756
CHOH757
CHOH758

site_idAC6
Number of Residues4
Detailsbinding site for residue PE3 C 602
ChainResidue
CASN439
CLYS440
CPE3601
CPE3603

site_idAC7
Number of Residues2
Detailsbinding site for residue PE3 C 603
ChainResidue
CPE3601
CPE3602

site_idAC8
Number of Residues1
Detailsbinding site for residue PE3 F 601
ChainResidue
FTHR312

Functional Information from PROSITE/UniProt
site_idPS00599
Number of Residues10
DetailsAA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TLGKSFGSVG
ChainResidueDetails
ATHR334-GLY343
BTHR334-GLY343

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P18079
ChainResidueDetails
BLLP337
CLLP337
FLLP337

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P18079
ChainResidueDetails
FARG91
FSER204
FLYS223
FTHR366
FTHR367
FTHR452
BARG91
BSER204
BLYS223
BTHR366
BTHR367
BTHR452
CARG91
CSER204
CLYS223
CTHR366
CTHR367
CTHR452

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P18079
ChainResidueDetails
BSER256
BHIS284
BTHR334
CSER256
CHIS284
CTHR334
FSER256
FHIS284
FTHR334

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:P18079
ChainResidueDetails
BLLP337
CLLP337
FLLP337

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PDB entries from 2024-05-15

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