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1L5F

Crystal Structure of CobT complexed with benzimidazole

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0008939molecular_functionnicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity
A0009236biological_processcobalamin biosynthetic process
A0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 992
ChainResidue
AALA78
AHOH463
AALA178
AASN179
ATHR180
AGLY202
AALA203
AHOH403
AHOH407
AHOH422

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 991
ChainResidue
AGLY264
APHE265
ALEU266
ASER291
AARG314
ALEU315
AGLY316
AHOH402
AHOH432

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BZI A 990
ChainResidue
APRO32
AVAL84
AGLN88
AGLU317

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:11441022
ChainResidueDetails
AGLN88

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:24121107, ECO:0000269|DOI:10.1074/jbc.M203535200
ChainResidueDetails
AALA203
APHE265
ASER291
AARG314
AGLU174

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important for substrate positioning, might be proton acceptor => ECO:0000269|PubMed:24121107
ChainResidueDetails
AGLU174

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for substrate positioning, might be proton acceptor => ECO:0000269|PubMed:24121107, ECO:0000305|PubMed:10587435, ECO:0000305|DOI:10.1074/jbc.M203535200
ChainResidueDetails
AGLU317

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 79
ChainResidueDetails
AGLU174electrostatic stabiliser, unknown
AGLU317activator, hydrogen bond acceptor, proton acceptor, unknown

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PDB entries from 2024-06-12

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