Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4DU6

Crystal structure of GTP cyclohydrolase I from Yersinia pestis complexed with GTP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003934	molecular_function	GTP cyclohydrolase I activity
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0006729	biological_process	tetrahydrobiopterin biosynthetic process
A	0006730	biological_process	one-carbon metabolic process
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0046654	biological_process	tetrahydrofolate biosynthetic process
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0003934	molecular_function	GTP cyclohydrolase I activity
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0006729	biological_process	tetrahydrobiopterin biosynthetic process
B	0006730	biological_process	one-carbon metabolic process
B	0008270	molecular_function	zinc ion binding
B	0016787	molecular_function	hydrolase activity
B	0046654	biological_process	tetrahydrofolate biosynthetic process
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0003934	molecular_function	GTP cyclohydrolase I activity
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0006729	biological_process	tetrahydrobiopterin biosynthetic process
C	0006730	biological_process	one-carbon metabolic process
C	0008270	molecular_function	zinc ion binding
C	0016787	molecular_function	hydrolase activity
C	0046654	biological_process	tetrahydrofolate biosynthetic process
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0003934	molecular_function	GTP cyclohydrolase I activity
D	0005525	molecular_function	GTP binding
D	0005737	cellular_component	cytoplasm
D	0006729	biological_process	tetrahydrobiopterin biosynthetic process
D	0006730	biological_process	one-carbon metabolic process
D	0008270	molecular_function	zinc ion binding
D	0016787	molecular_function	hydrolase activity
D	0046654	biological_process	tetrahydrofolate biosynthetic process
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0003934	molecular_function	GTP cyclohydrolase I activity
E	0005525	molecular_function	GTP binding
E	0005737	cellular_component	cytoplasm
E	0006729	biological_process	tetrahydrobiopterin biosynthetic process
E	0006730	biological_process	one-carbon metabolic process
E	0008270	molecular_function	zinc ion binding
E	0016787	molecular_function	hydrolase activity
E	0046654	biological_process	tetrahydrofolate biosynthetic process
E	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE GTP A 301

Chain	Residue
A	THR86
B	CYS109
B	HIS111
B	HIS112
B	VAL149
B	GLN150
B	GLU151
B	HIS178
B	CYS180
B	ARG184
B	CA305
A	VAL130
C	ARG64
A	ILE131
A	GLY132
A	LEU133
A	SER134
A	LYS135
A	ARG138
A	HOH426

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 302

Chain	Residue
A	GLN155
A	LEU158
A	SER197
A	LEU198
A	LYS203
E	LYS93
E	ASP95
E	GLU96

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL B 301

Chain	Residue
A	LYS93
A	ASP95
A	GLU96
A	HOH428
B	GLN155
B	SER197
B	LEU198
B	LYS203
B	PEG302
B	HOH411
B	HOH435

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PEG B 302

Chain	Residue
B	ARG18
B	LEU20
B	GLN155
B	LEU158
B	LEU159
B	GLN162
B	GLY199
B	GOL301
B	HOH404
B	HOH411
B	HOH417
B	HOH428

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE TRS B 303

Chain	Residue
B	HIS12
B	LEU16
B	LEU24
B	LYS26
B	HOH421

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE GTP B 304

Chain	Residue
B	ARG64
B	THR86
B	VAL130
B	ILE131
B	GLY132
B	LEU133
B	SER134
B	LYS135
B	ARG138
C	HIS111
C	HIS112
C	VAL149
C	GLN150
C	GLU151
C	HIS178
C	CYS180
C	ARG184
C	CA304

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 305

Chain	Residue
A	GTP301
B	CYS109
B	HIS111
B	HIS112
B	CYS180

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 301

Chain	Residue
B	ASP95
B	GLU96
C	GLN155
C	SER197
C	LEU198
C	LYS203
C	HOH443

site_id	AC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE GTP C 302

Chain	Residue
D	HIS111
D	HIS112
D	VAL149
D	GLN150
D	GLU151
D	HIS178
D	CYS180
D	ARG184
D	GLY185
D	CA304
D	HOH422
A	ARG64
C	LYS84
C	THR86
C	VAL130
C	ILE131
C	GLY132
C	LEU133
C	SER134
C	LYS135
C	ARG138
C	HOH421
C	HOH436
D	CYS109

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE TRS C 303

Chain	Residue
C	HIS12
C	LEU16
C	LEU24
C	LYS26

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 304

Chain	Residue
B	GTP304
C	CYS109
C	HIS111
C	HIS112
C	CYS180

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 305

Chain	Residue
A	ARG37
B	HIS41
C	ARG37
D	HIS47

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 306

Chain	Residue
C	ASP117
C	LYS119
C	ASP175
C	VAL177

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 301

Chain	Residue
C	LYS93
C	ASP95
C	GLU96
D	GLN155
D	LEU158
D	LEU198
D	LYS203

site_id	BC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE GTP D 302

Chain	Residue
D	THR86
D	VAL130
D	ILE131
D	GLY132
D	LEU133
D	SER134
D	LYS135
D	ARG138
E	ARG64
E	CYS109
E	HIS111
E	HIS112
E	VAL149
E	GLN150
E	GLU151
E	HIS178
E	CYS180
E	ARG184

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE TRS D 303

Chain	Residue
D	HIS12
D	LEU16
D	LEU24
D	ARG25
D	LYS26
D	HOH420

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 304

Chain	Residue
C	GTP302
D	CYS109
D	HIS111
D	HIS112
D	CYS180

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL E 301

Chain	Residue
D	ASP95
D	GLU96
E	GLN155
E	LEU158
E	SER197
E	LEU198
E	LYS203

site_id	CC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE GTP E 302

Chain	Residue
A	CYS109
A	HIS111
A	HIS112
A	VAL149
A	GLN150
A	GLU151
A	HIS178
A	CYS180
A	ARG184
A	HOH434
D	ARG64
E	THR86
E	VAL130
E	ILE131
E	GLY132
E	LEU133
E	SER134
E	LYS135
E	ARG138
E	HOH414

Functional Information from PROSITE/UniProt

site_id	PS00859
Number of Residues	17
Details	GTP_CYCLOHYDROL_1_1 GTP cyclohydrolase I signature 1. EMVtvRDItltStCEHH

Chain	Residue	Details
A	GLU96-HIS112

site_id	PS00860
Number of Residues	11
Details	GTP_CYCLOHYDROL_1_2 GTP cyclohydrolase I signature 2. AqRpQVQERLT

Chain	Residue	Details
A	ALA144-THR154

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00223","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)