1IBV

STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT-170 C

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004398	molecular_function	histidine decarboxylase activity
A	0006520	biological_process	amino acid metabolic process
A	0006547	biological_process	L-histidine metabolic process
A	0016831	molecular_function	carboxy-lyase activity
B	0004398	molecular_function	histidine decarboxylase activity
B	0006520	biological_process	amino acid metabolic process
B	0006547	biological_process	L-histidine metabolic process
B	0016831	molecular_function	carboxy-lyase activity
C	0004398	molecular_function	histidine decarboxylase activity
C	0006520	biological_process	amino acid metabolic process
C	0006547	biological_process	L-histidine metabolic process
C	0016831	molecular_function	carboxy-lyase activity
D	0004398	molecular_function	histidine decarboxylase activity
D	0006520	biological_process	amino acid metabolic process
D	0006547	biological_process	L-histidine metabolic process
D	0016831	molecular_function	carboxy-lyase activity
E	0004398	molecular_function	histidine decarboxylase activity
E	0006520	biological_process	amino acid metabolic process
E	0006547	biological_process	L-histidine metabolic process
E	0016831	molecular_function	carboxy-lyase activity
F	0004398	molecular_function	histidine decarboxylase activity
F	0006520	biological_process	amino acid metabolic process
F	0006547	biological_process	L-histidine metabolic process
F	0016831	molecular_function	carboxy-lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PYR B 483

Chain	Residue
A	SER81
B	PHE484
B	MET595
B	PHE596
B	PVH801
C	ASN76

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PYR D 483

Chain	Residue
D	PHE596
D	PVH801
E	ASN76
C	SER81
D	PHE484
D	MET595

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PYR F 483

Chain	Residue
A	ASN76
E	SER81
F	PHE484
F	MET595
F	PHE596
F	PVH801

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site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PVH B 801

Chain	Residue
A	ALA80
A	SER81
B	PYR483
B	PHE484
B	ASN555
B	LYS556
B	PHE596
B	VAL597
B	GLU598
C	ASP63
C	GLU66

---

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PVH D 801

Chain	Residue
C	ALA80
C	SER81
D	PYR483
D	PHE484
D	LYS556
D	PHE596
D	VAL597
D	GLU598
E	ASP63
E	GLU66
E	HOH108

---

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PVH F 801

Chain	Residue
A	ASP63
A	GLU66
E	ALA80
E	SER81
F	PYR483
F	PHE484
F	LYS556
F	PHE596
F	VAL597
F	GLU598
F	HOH904

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton donor

Chain	Residue	Details
B	GLU598
D	GLU598
F	GLU598
C	SER81
E	ASP63
E	SER81

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site_id	SWS_FT_FI2
Number of Residues	3
Details	MOD_RES: Pyruvic acid (Ser) => ECO:0000269|PubMed:6698997

Chain	Residue	Details
B	PYR483
D	PYR483
F	PYR483

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Catalytic Information from CSA

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

Chain	Residue	Details
A	TYR62

---

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

Chain	Residue	Details
E	SER81

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site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1pya

Chain	Residue	Details
A	SER81
C	TYR62
B	PHE195
B	GLU197

---

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1pya

Chain	Residue	Details
C	SER81
D	PHE195
D	GLU197
E	TYR62

---

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1pya

Chain	Residue	Details
F	PHE195
F	GLU197

---

site_id	MCSA1
Number of Residues	3
Details	M-CSA 49

Chain	Residue	Details
B	PYR483	covalently attached, electrofuge, electron pair acceptor, electron pair donor, electrophile, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	PHE596	electrostatic stabiliser, hydrogen bond donor
B	GLU598	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	SER81	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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site_id	MCSA2
Number of Residues	3
Details	M-CSA 49

Chain	Residue	Details
D	PYR483	covalently attached, electrofuge, electron pair acceptor, electron pair donor, electrophile, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	PHE596	electrostatic stabiliser, hydrogen bond donor
D	GLU598	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	SER81	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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site_id	MCSA3
Number of Residues	3
Details	M-CSA 49

Chain	Residue	Details
F	PYR483	covalently attached, electrofuge, electron pair acceptor, electron pair donor, electrophile, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
F	PHE596	electrostatic stabiliser, hydrogen bond donor
F	GLU598	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	SER81	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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