1HXD

CRYSTAL STRUCTURE OF E. COLI BIOTIN REPRESSOR WITH BOUND BIOTIN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000976	molecular_function	transcription cis-regulatory region binding
A	0003676	molecular_function	nucleic acid binding
A	0003677	molecular_function	DNA binding
A	0004077	molecular_function	biotin--[biotin carboxyl-carrier protein] ligase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006768	biological_process	biotin metabolic process
A	0009102	biological_process	biotin biosynthetic process
A	0009374	molecular_function	biotin binding
A	0016874	molecular_function	ligase activity
A	0017053	cellular_component	transcription repressor complex
A	0036211	biological_process	protein modification process
A	0042803	molecular_function	protein homodimerization activity
B	0000166	molecular_function	nucleotide binding
B	0000976	molecular_function	transcription cis-regulatory region binding
B	0003676	molecular_function	nucleic acid binding
B	0003677	molecular_function	DNA binding
B	0004077	molecular_function	biotin--[biotin carboxyl-carrier protein] ligase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006355	biological_process	regulation of DNA-templated transcription
B	0006768	biological_process	biotin metabolic process
B	0009102	biological_process	biotin biosynthetic process
B	0009374	molecular_function	biotin binding
B	0016874	molecular_function	ligase activity
B	0017053	cellular_component	transcription repressor complex
B	0036211	biological_process	protein modification process
B	0042803	molecular_function	protein homodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE BTN A 500

Chain	Residue
A	SER89
A	SER134
A	LYS183
A	GLY186
A	ILE187
A	LEU188
A	GLY204
A	ALA205
A	GLY206
A	THR90
A	ASN91
A	GLN112
A	ARG116
A	GLY117
A	ARG118
A	TRP123
A	LEU133

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site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE BTN B 501

Chain	Residue
B	SER89
B	THR90
B	GLN112
B	GLY115
B	ARG116
B	GLY117
B	ARG118
B	ARG121
B	TRP123
B	TYR132
B	LYS183
B	GLY186
B	ILE187
B	LEU188
B	ALA205
B	GLY206

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	38
Details	DNA binding: {"description":"H-T-H motif","evidences":[{"source":"HAMAP-Rule","id":"MF_00978","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00978","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11353844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1409631","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 538

Chain	Residue	Details
A	ARG118	electrostatic stabiliser
A	LYS183	electrostatic stabiliser
A	ARG317

---

site_id	MCSA2
Number of Residues	3
Details	M-CSA 538

Chain	Residue	Details
B	ARG118	electrostatic stabiliser
B	LYS183	electrostatic stabiliser
B	ARG317

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