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1QGO

ANAEROBIC COBALT CHELATASE IN COBALAMIN BIOSYNTHESIS FROM SALMONELLA TYPHIMURIUM

Functional Information from GO Data
ChainGOidnamespacecontents
A0006779biological_processporphyrin-containing compound biosynthetic process
A0009236biological_processcobalamin biosynthetic process
A0016829molecular_functionlyase activity
A0016852molecular_functionsirohydrochlorin cobaltochelatase activity
A0019251biological_processanaerobic cobalamin biosynthetic process
A0046872molecular_functionmetal ion binding
A0046906molecular_functiontetrapyrrole binding
A0050897molecular_functioncobalt ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 400
ChainResidue
AHOH646
AHOH675
AHOH714
AGLY87
AASP88
AGLU89
ASER148
AHIS150
AHOH584
AHOH640

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AVAL174
AGLU175
AVAL180
ATRP220
AARG223
AHOH555
AHOH695
AHOH702

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AGLN64
ALYS221
APRO233
AHOH568
AHOH667

site_idCO
Number of Residues2
DetailsTHE ACTIVE SITE IS LOCATED IN A CLEFT BETWEEN THE TWO DOMAINS SURROUNDED BY FOUR REGIONS OF STRUCTURE COMPRISED RESPECTIVELY BY RESIDUES 10-14, 86-89, 145- 149, 205-207. HIS 145 AND HIS 207 ARE THE TWO RESIDUES SHOWN TO BE RESPONSIBLE FOR METAL BINDING.
ChainResidue
AHIS145
AHIS207

Functional Information from PROSITE/UniProt
site_idPS00761
Number of Residues14
DetailsSPASE_I_3 Signal peptidases I signature 3. MLVAGDHAinDmaS
ChainResidueDetails
AMET201-SER214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:21173279
ChainResidueDetails
AHIS145

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:21173279, ECO:0007744|PDB:2XWP
ChainResidueDetails
AGLY45
AILE84
AILE85
AASP88
AGLU89
ALYS92
ALEU202
AVAL203
AHIS207

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q72EC8
ChainResidueDetails
AHIS145
AGLU175

226707

PDB entries from 2024-10-30

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