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5MHB

Product-Complex of E.coli 5-Amino Laevulinic Acid Dehydratase

Replaces:  5IC2
Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004655molecular_functionporphobilinogen synthase activity
A0005829cellular_componentcytosol
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0006783biological_processheme biosynthetic process
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0033014biological_processtetrapyrrole biosynthetic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue PBG A 401
ChainResidue
ACYS120
ALYS247
ATYR270
AVAL272
ASER273
ATYR312
AZN403
AHOH522
ACYS122
ASER165
ALYS195
ATYR201
APHE204
AARG205
AARG216
AGLN220

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 402
ChainResidue
AGLU40
AGLU40
AHIS84
AHIS84

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 403
ChainResidue
ACYS120
ACYS122
ACYS130
APBG401

site_idAC4
Number of Residues6
Detailsbinding site for residue ZN A 404
ChainResidue
AGLU232
AHOH516
AHOH535
AHOH560
AHOH584
AHOH740

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL A 405
ChainResidue
ALEU295
AGLU296
AHOH591

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 406
ChainResidue
AGLU290
AGLU291
APHE313
AASP316
ALYS320
AILE322
AHOH669

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL A 407
ChainResidue
AALA197
ASER199
AASP215
AARG216
ALYS217
AHOH530

Functional Information from PROSITE/UniProt
site_idPS00169
Number of Residues13
DetailsD_ALA_DEHYDRATASE Delta-aminolevulinic acid dehydratase active site. GaDcLMVKPAgaY
ChainResidueDetails
AGLY240-TYR252

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate
ChainResidueDetails
ALYS195
ALYS247

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11444968, ECO:0000269|PubMed:11909869
ChainResidueDetails
ACYS120
ACYS122
ACYS130
AGLU232

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AARG205
AARG216
ASER273
ATYR312

226707

PDB entries from 2024-10-30

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