Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2O7B

Tyrosine ammonia-lyase from Rhodobacter sphaeroides, complexed with coumarate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0006572	biological_process	tyrosine catabolic process
A	0009698	biological_process	phenylpropanoid metabolic process
A	0009699	biological_process	phenylpropanoid biosynthetic process
A	0016829	molecular_function	lyase activity
A	0016841	molecular_function	ammonia-lyase activity
A	0042802	molecular_function	identical protein binding
A	0044550	biological_process	secondary metabolite biosynthetic process
A	0045548	molecular_function	phenylalanine ammonia-lyase activity
A	0051289	biological_process	protein homotetramerization
A	0052883	molecular_function	tyrosine ammonia-lyase activity
B	0003824	molecular_function	catalytic activity
B	0006572	biological_process	tyrosine catabolic process
B	0009698	biological_process	phenylpropanoid metabolic process
B	0009699	biological_process	phenylpropanoid biosynthetic process
B	0016829	molecular_function	lyase activity
B	0016841	molecular_function	ammonia-lyase activity
B	0042802	molecular_function	identical protein binding
B	0044550	biological_process	secondary metabolite biosynthetic process
B	0045548	molecular_function	phenylalanine ammonia-lyase activity
B	0051289	biological_process	protein homotetramerization
B	0052883	molecular_function	tyrosine ammonia-lyase activity
C	0003824	molecular_function	catalytic activity
C	0006572	biological_process	tyrosine catabolic process
C	0009698	biological_process	phenylpropanoid metabolic process
C	0009699	biological_process	phenylpropanoid biosynthetic process
C	0016829	molecular_function	lyase activity
C	0016841	molecular_function	ammonia-lyase activity
C	0042802	molecular_function	identical protein binding
C	0044550	biological_process	secondary metabolite biosynthetic process
C	0045548	molecular_function	phenylalanine ammonia-lyase activity
C	0051289	biological_process	protein homotetramerization
C	0052883	molecular_function	tyrosine ammonia-lyase activity
D	0003824	molecular_function	catalytic activity
D	0006572	biological_process	tyrosine catabolic process
D	0009698	biological_process	phenylpropanoid metabolic process
D	0009699	biological_process	phenylpropanoid biosynthetic process
D	0016829	molecular_function	lyase activity
D	0016841	molecular_function	ammonia-lyase activity
D	0042802	molecular_function	identical protein binding
D	0044550	biological_process	secondary metabolite biosynthetic process
D	0045548	molecular_function	phenylalanine ammonia-lyase activity
D	0051289	biological_process	protein homotetramerization
D	0052883	molecular_function	tyrosine ammonia-lyase activity
E	0003824	molecular_function	catalytic activity
E	0006572	biological_process	tyrosine catabolic process
E	0009698	biological_process	phenylpropanoid metabolic process
E	0009699	biological_process	phenylpropanoid biosynthetic process
E	0016829	molecular_function	lyase activity
E	0016841	molecular_function	ammonia-lyase activity
E	0042802	molecular_function	identical protein binding
E	0044550	biological_process	secondary metabolite biosynthetic process
E	0045548	molecular_function	phenylalanine ammonia-lyase activity
E	0051289	biological_process	protein homotetramerization
E	0052883	molecular_function	tyrosine ammonia-lyase activity
F	0003824	molecular_function	catalytic activity
F	0006572	biological_process	tyrosine catabolic process
F	0009698	biological_process	phenylpropanoid metabolic process
F	0009699	biological_process	phenylpropanoid biosynthetic process
F	0016829	molecular_function	lyase activity
F	0016841	molecular_function	ammonia-lyase activity
F	0042802	molecular_function	identical protein binding
F	0044550	biological_process	secondary metabolite biosynthetic process
F	0045548	molecular_function	phenylalanine ammonia-lyase activity
F	0051289	biological_process	protein homotetramerization
F	0052883	molecular_function	tyrosine ammonia-lyase activity
G	0003824	molecular_function	catalytic activity
G	0006572	biological_process	tyrosine catabolic process
G	0009698	biological_process	phenylpropanoid metabolic process
G	0009699	biological_process	phenylpropanoid biosynthetic process
G	0016829	molecular_function	lyase activity
G	0016841	molecular_function	ammonia-lyase activity
G	0042802	molecular_function	identical protein binding
G	0044550	biological_process	secondary metabolite biosynthetic process
G	0045548	molecular_function	phenylalanine ammonia-lyase activity
G	0051289	biological_process	protein homotetramerization
G	0052883	molecular_function	tyrosine ammonia-lyase activity
H	0003824	molecular_function	catalytic activity
H	0006572	biological_process	tyrosine catabolic process
H	0009698	biological_process	phenylpropanoid metabolic process
H	0009699	biological_process	phenylpropanoid biosynthetic process
H	0016829	molecular_function	lyase activity
H	0016841	molecular_function	ammonia-lyase activity
H	0042802	molecular_function	identical protein binding
H	0044550	biological_process	secondary metabolite biosynthetic process
H	0045548	molecular_function	phenylalanine ammonia-lyase activity
H	0051289	biological_process	protein homotetramerization
H	0052883	molecular_function	tyrosine ammonia-lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HC4 A 701

Chain	Residue
A	TYR60
D	TYR300
D	ARG303
A	GLY67
A	HIS89
A	LEU90
A	ASN432
A	ASN435
A	GLN436
B	MET405
B	GLY406

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HC4 B 701

Chain	Residue
A	MET405
B	TYR60
B	GLY67
B	HIS89
B	LEU90
B	ASN432
B	ASN435
B	GLN436
B	HOH5255
C	TYR300
C	ARG303

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE HC4 C 701

Chain	Residue
B	TYR300
B	ARG303
C	TYR60
C	GLY67
C	HIS89
C	LEU90
C	ASN432
C	ASN435
C	GLN436
D	MET405

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE HC4 D 701

Chain	Residue
A	TYR300
A	ARG303
C	MET405
D	TYR60
D	GLY67
D	HIS89
D	LEU90
D	ASN432
D	ASN435
D	GLN436

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HC4 E 701

Chain	Residue
E	TYR60
E	GLY67
E	HIS89
E	LEU90
E	ASN432
E	ASN435
E	GLN436
E	HOH4924
E	HOH5112
F	MET405
H	TYR300
H	ARG303

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HC4 F 701

Chain	Residue
E	MET405
F	TYR60
F	GLY67
F	HIS89
F	LEU90
F	ASN432
F	ASN435
F	GLN436
F	HOH5116
G	TYR300
G	ARG303

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HC4 G 701

Chain	Residue
F	TYR300
F	ARG303
G	TYR60
G	GLY67
G	HIS89
G	LEU90
G	LEU153
G	ASN432
G	ASN435
G	GLN436
G	HOH5238
H	MET405

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HC4 H 701

Chain	Residue
E	TYR300
E	ARG303
G	MET405
H	TYR60
H	GLY67
H	HIS89
H	LEU90
H	ASN432
H	ASN435
H	GLN436
H	HOH2960

Functional Information from PROSITE/UniProt

site_id	PS00488
Number of Residues	17
Details	PAL_HISTIDASE Phenylalanine and histidine ammonia-lyases signature. GTVGASGDLtPLAhmvL

Chain	Residue	Details
A	GLY145-LEU163

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250

Chain	Residue	Details
A	TYR60
B	TYR60
C	TYR60
D	TYR60
E	TYR60
F	TYR60
G	TYR60
H	TYR60

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING:

Chain	Residue	Details
A	HIS89
D	HIS89
D	ALA305
D	ALA434
E	HIS89
E	ALA305
E	ALA434
F	HIS89
F	ALA305
F	ALA434
G	HIS89
A	ALA305
G	ALA305
G	ALA434
H	HIS89
H	ALA305
H	ALA434
A	ALA434
B	HIS89
B	ALA305
B	ALA434
C	HIS89
C	ALA305
C	ALA434

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: 2,3-didehydroalanine (Ser) => ECO:0000305\|PubMed:17185228

Chain	Residue	Details
A	ASP152
B	ASP152
C	ASP152
D	ASP152
E	ASP152
F	ASP152
G	ASP152
H	ASP152

site_id	SWS_FT_FI4
Number of Residues	16
Details	CROSSLNK: 5-imidazolinone (Ala-Gly) => ECO:0000305\|PubMed:17185228

Chain	Residue	Details
A	MDO149
E	LEU153
F	MDO149
F	LEU153
G	MDO149
G	LEU153
H	MDO149
H	LEU153
A	LEU153
B	MDO149
B	LEU153
C	MDO149
C	LEU153
D	MDO149
D	LEU153
E	MDO149

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