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1JHP

Three-dimensional Structure of CobT in Complex with 5-methoxybenzimidazole

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 Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 991
ChainResidue
AGLY264
APHE265
ALEU266
ASER291
AARG314
ALEU315
AGLY316
AHOH1002

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 992
ChainResidue
AALA178
AASN179
ATHR180
AGLY202
AALA203
AHOH1027
AHOH1028
AHOH1064
AALA78

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 5OB A 990
ChainResidue
APRO32
ASER80
AGLN88
ALEU315
AGLU317
ALEU348

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
AGLU174
AALA203
APHE265
ASER291
AARG314

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_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1d0s
ChainResidueDetails
AGLU317

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 2024-07-17

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