1L4K

Crystal Structure of CobT complexed with 3,4-dimethylaniline and nicotinate mononucleotide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0008939	molecular_function	nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity
A	0009236	biological_process	cobalamin biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 34A A 990

Chain	Residue
A	PRO32
A	SER80
A	GLN88
A	LEU315
A	GLU317

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site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NCN A 991

Chain	Residue
A	ALA178
A	ASN179
A	THR180
A	GLY202
A	ALA203
A	PHE265
A	LEU266
A	SER291
A	GLU293
A	ARG314
A	LEU315
A	GLY316
A	HOH1005
A	HOH1019
A	HOH1023
A	ALA78
A	GLU174
A	GLY176
A	MET177

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305|PubMed:11441022

Chain	Residue	Details
A	GLN88

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:24121107, ECO:0000269|DOI:10.1074/jbc.M203535200

Chain	Residue	Details
A	GLU174
A	ALA203
A	PHE265
A	SER291
A	ARG314

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site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Important for substrate positioning, might be proton acceptor => ECO:0000269|PubMed:24121107

Chain	Residue	Details
A	GLU174

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Important for substrate positioning, might be proton acceptor => ECO:0000269|PubMed:24121107, ECO:0000305|PubMed:10587435, ECO:0000305|DOI:10.1074/jbc.M203535200

Chain	Residue	Details
A	GLU317

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 79

Chain	Residue	Details
A	GLU174	electrostatic stabiliser, unknown
A	GLU317	activator, hydrogen bond acceptor, proton acceptor, unknown

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