1JHR

Three-dimensional Structure of CobT in Complex with Reaction Products of 2-hydroxypurine and NaMN

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	0016757	molecular_function	glycosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE NIO A 991

Chain	Residue
A	GLY264
A	HOH1018
A	PHE265
A	LEU266
A	SER291
A	ARG314
A	LEU315
A	GLY316
A	P2P990
A	HOH1003

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site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE P2P A 990

Chain	Residue
A	ALA78
A	VAL84
A	GLN88
A	GLU174
A	LEU175
A	GLY176
A	MET177
A	ALA178
A	ASN179
A	THR180
A	GLY202
A	ALA203
A	LEU315
A	GLU317
A	NIO991
A	HOH1011
A	HOH1017
A	HOH1021
A	HOH1040

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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	ALA203
A	PHE265
A	SER291
A	ARG314
A	GLU174

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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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