Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1KH3

Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000050	biological_process	urea cycle
A	0000053	biological_process	argininosuccinate metabolic process
A	0000166	molecular_function	nucleotide binding
A	0004055	molecular_function	argininosuccinate synthase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006526	biological_process	L-arginine biosynthetic process
A	0008652	biological_process	amino acid biosynthetic process
A	0016874	molecular_function	ligase activity
B	0000050	biological_process	urea cycle
B	0000053	biological_process	argininosuccinate metabolic process
B	0000166	molecular_function	nucleotide binding
B	0004055	molecular_function	argininosuccinate synthase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006526	biological_process	L-arginine biosynthetic process
B	0008652	biological_process	amino acid biosynthetic process
B	0016874	molecular_function	ligase activity
C	0000050	biological_process	urea cycle
C	0000053	biological_process	argininosuccinate metabolic process
C	0000166	molecular_function	nucleotide binding
C	0004055	molecular_function	argininosuccinate synthase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006526	biological_process	L-arginine biosynthetic process
C	0008652	biological_process	amino acid biosynthetic process
C	0016874	molecular_function	ligase activity
D	0000050	biological_process	urea cycle
D	0000053	biological_process	argininosuccinate metabolic process
D	0000166	molecular_function	nucleotide binding
D	0004055	molecular_function	argininosuccinate synthase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006526	biological_process	L-arginine biosynthetic process
D	0008652	biological_process	amino acid biosynthetic process
D	0016874	molecular_function	ligase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 540

Chain	Residue
A	SER8
A	GLY10
A	LEU11
A	ASP12
A	THR13
A	ANP510

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 4540

Chain	Residue
B	THR13
B	HOH1373
B	ANP4510
B	SER8
B	GLY10
B	ASP12

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 2540

Chain	Residue
C	SER8
C	GLY10
C	LEU11
C	ASP12
C	THR13
C	ANP2510

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 3540

Chain	Residue
D	SER8
D	GLY10
D	LEU11
D	ASP12
D	THR13
D	ANP3510

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 550

Chain	Residue
A	ANP510
A	HOH1001
A	HOH1005
A	HOH1006

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 4550

Chain	Residue
A	HOH1008
B	HOH1002
B	HOH1007
B	ANP4510

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 2550

Chain	Residue
C	HOH1003
C	HOH1009
C	HOH1010
C	ANP2510

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 3550

Chain	Residue
D	HOH1004
D	HOH1011
D	HOH1012
D	ANP3510

site_id	AC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ANP A 510

Chain	Residue
A	ALA6
A	THR13
A	PHE31
A	THR32
A	ALA33
A	GLN37
A	ARG92
A	HIS113
A	GLY114
A	PHE125
A	SER173
A	MET174
A	ARG520
A	ASP530
A	SO4540
A	MG550
A	HOH1005
A	HOH1494
A	HOH1536

site_id	BC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ANP B 4510

Chain	Residue
A	HOH1008
A	ARG4520
A	ASP4530
B	ALA6
B	TYR7
B	THR13
B	PHE31
B	THR32
B	ALA33
B	GLN37
B	ARG92
B	HIS113
B	GLY114
B	PHE125
B	SER173
B	MET174
B	HOH1237
B	HOH1396
B	HOH1501
B	SO44540
B	MG4550

site_id	BC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ANP C 2510

Chain	Residue
A	ARG2520
A	ASP2530
C	ALA6
C	THR13
C	PHE31
C	THR32
C	ALA33
C	GLN37
C	ARG92
C	HIS113
C	GLY114
C	PHE125
C	SER173
C	MET174
C	HOH1010
C	HOH1440
C	SO42540
C	MG2550

site_id	BC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ANP D 3510

Chain	Residue
A	ASP3530
D	ALA6
D	TYR7
D	THR13
D	PHE31
D	ALA33
D	GLN37
D	ARG92
D	HIS113
D	GLY114
D	PHE125
D	SER173
D	MET174
D	HOH1004
D	SO43540
D	MG3550
A	ARG3520

site_id	BC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ARG A 520

Chain	Residue
A	TYR84
A	THR88
A	SER89
A	ASN120
A	ARG124
A	SER173
A	MET174
A	ASP175
A	SER182
A	TYR183
A	GLU184
A	GLU258
A	TYR270
A	TYR310
A	ANP510
A	HOH1013

site_id	BC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ARG A 4520

Chain	Residue
A	HOH1038
B	TYR84
B	THR88
B	SER89
B	ASN120
B	ARG124
B	SER173
B	MET174
B	ASP175
B	SER182
B	GLU184
B	GLU258
B	TYR270
B	TYR310
B	ANP4510

site_id	BC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ARG A 2520

Chain	Residue
A	HOH1042
C	TYR84
C	THR88
C	SER89
C	ASN120
C	ARG124
C	SER173
C	MET174
C	ASP175
C	SER182
C	GLU184
C	GLU258
C	TYR270
C	TYR310
C	ANP2510

site_id	BC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ARG A 3520

Chain	Residue
A	HOH1156
D	TYR84
D	THR88
D	SER89
D	ASN120
D	ARG124
D	SER173
D	MET174
D	ASP175
D	SER182
D	GLU184
D	GLU258
D	TYR270
D	TYR310
D	ANP3510

site_id	BC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ASP A 530

Chain	Residue
A	ALA115
A	THR116
A	GLY119
A	ASN120
A	ASP121
A	ANP510
A	HOH1005
A	HOH1013
A	HOH1039
A	HOH1244

site_id	BC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ASP A 4530

Chain	Residue
A	HOH1008
A	HOH1038
A	HOH1409
B	ALA115
B	THR116
B	GLY119
B	ASN120
B	ASP121
B	HOH1090
B	ANP4510

site_id	CC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ASP A 2530

Chain	Residue
A	HOH1042
A	HOH1291
C	ALA115
C	THR116
C	GLY119
C	ASN120
C	ASP121
C	HOH1010
C	HOH1067
C	ANP2510

site_id	CC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ASP A 3530

Chain	Residue
A	HOH1156
A	HOH1229
D	ALA115
D	THR116
D	GLY119
D	ASN120
D	ASP121
D	GLU184
D	HOH1004
D	HOH1137
D	ANP3510

Functional Information from PROSITE/UniProt

site_id	PS00564
Number of Residues	9
Details	ARGININOSUCCIN_SYN_1 Argininosuccinate synthase signature 1. AYSGGLDTS

Chain	Residue	Details
A	ALA6-SER14

site_id	PS00565
Number of Residues	12
Details	ARGININOSUCCIN_SYN_2 Argininosuccinate synthase signature 2. GaTgKGNDqvRF

Chain	Residue	Details
A	GLY114-PHE125

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00005","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11844799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12684518","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	40
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1kp2

Chain	Residue	Details
A	ASP121
A	ARG92

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1kp2

Chain	Residue	Details
B	ASP121
B	ARG92

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1kp2

Chain	Residue	Details
C	ASP121
C	ARG92

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1kp2

Chain	Residue	Details
D	ASP121
D	ARG92

site_id	MCSA1
Number of Residues	4
Details	M-CSA 316

Chain	Residue	Details
A	ASP12	steric role
A	ARG92	electrostatic stabiliser, hydrogen bond donor
A	ASP121	proton acceptor, proton donor
A	SER173	hydrogen bond donor, steric role

site_id	MCSA2
Number of Residues	4
Details	M-CSA 316

Chain	Residue	Details
B	ASP12	steric role
B	ARG92	electrostatic stabiliser, hydrogen bond donor
B	ASP121	proton acceptor, proton donor
B	SER173	hydrogen bond donor, steric role

site_id	MCSA3
Number of Residues	4
Details	M-CSA 316

Chain	Residue	Details
C	ASP12	steric role
C	ARG92	electrostatic stabiliser, hydrogen bond donor
C	ASP121	proton acceptor, proton donor
C	SER173	hydrogen bond donor, steric role

site_id	MCSA4
Number of Residues	4
Details	M-CSA 316

Chain	Residue	Details
D	ASP12	steric role
D	ARG92	electrostatic stabiliser, hydrogen bond donor
D	ASP121	proton acceptor, proton donor
D	SER173	hydrogen bond donor, steric role

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