1F2D

1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008660	molecular_function	1-aminocyclopropane-1-carboxylate deaminase activity
A	0009310	biological_process	amine catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016846	molecular_function	carbon-sulfur lyase activity
A	0019148	molecular_function	D-cysteine desulfhydrase activity
A	0030170	molecular_function	pyridoxal phosphate binding
B	0008660	molecular_function	1-aminocyclopropane-1-carboxylate deaminase activity
B	0009310	biological_process	amine catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016846	molecular_function	carbon-sulfur lyase activity
B	0019148	molecular_function	D-cysteine desulfhydrase activity
B	0030170	molecular_function	pyridoxal phosphate binding
C	0008660	molecular_function	1-aminocyclopropane-1-carboxylate deaminase activity
C	0009310	biological_process	amine catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016846	molecular_function	carbon-sulfur lyase activity
C	0019148	molecular_function	D-cysteine desulfhydrase activity
C	0030170	molecular_function	pyridoxal phosphate binding
D	0008660	molecular_function	1-aminocyclopropane-1-carboxylate deaminase activity
D	0009310	biological_process	amine catabolic process
D	0016787	molecular_function	hydrolase activity
D	0016846	molecular_function	carbon-sulfur lyase activity
D	0019148	molecular_function	D-cysteine desulfhydrase activity
D	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 940

Chain	Residue
A	LYS51
A	SER78
A	ASN79
A	GLN80
A	TYR295
A	PLP342
A	HOH1008

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 941

Chain	Residue
B	ASN79
B	GLN80
B	TYR269
B	TYR295
B	PLP342
B	HOH1025
B	LYS51
B	SER78

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 C 942

Chain	Residue
C	LYS51
C	SER78
C	ASN79
C	GLN80
C	TYR295
C	PLP342
C	HOH944
C	HOH951
C	HOH977

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 D 943

Chain	Residue
D	LYS51
D	SER78
D	ASN79
D	GLN80
D	TYR295
D	PLP342
D	HOH973
D	HOH981
D	HOH1002

---

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PLP A 342

Chain	Residue
A	ASN50
A	LYS51
A	LYS54
A	ASN79
A	SER166
A	CYS200
A	VAL201
A	THR202
A	GLY203
A	SER204
A	THR205
A	TYR295
A	GLU296
A	LEU323
A	GLY324
A	GLY325
A	SO4940
A	HOH1009
A	HOH1019

---

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP B 342

Chain	Residue
B	ASN50
B	LYS51
B	LYS54
B	ASN79
B	CYS200
B	VAL201
B	THR202
B	GLY203
B	THR205
B	TYR295
B	GLU296
B	LEU323
B	GLY324
B	GLY325
B	SO4941
B	HOH947
B	HOH1013

---

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PLP C 342

Chain	Residue
C	ASN50
C	LYS51
C	LYS54
C	ASN79
C	CYS200
C	VAL201
C	THR202
C	GLY203
C	THR205
C	TYR295
C	GLU296
C	LEU323
C	GLY324
C	GLY325
C	SO4942
C	HOH977
C	HOH1078
C	HOH1080

---

site_id	AC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PLP D 342

Chain	Residue
D	LEU323
D	GLY324
D	GLY325
D	SO4943
D	HOH953
D	HOH981
D	HOH1061
D	ASN50
D	LYS51
D	LYS54
D	ASN79
D	CYS200
D	VAL201
D	THR202
D	GLY203
D	SER204
D	THR205
D	TYR295
D	GLU296

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Nucleophile

Chain	Residue	Details
A	SER78
B	SER78
C	SER78
D	SER78

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: N-acetylserine => ECO:0000269|PubMed:9604000

Chain	Residue	Details
A	ALA1
B	ALA1
C	ALA1
D	ALA1

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: N6-(pyridoxal phosphate)lysine

Chain	Residue	Details
A	LYS51
B	LYS51
C	LYS51
D	LYS51

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 15491139, 16524684

Chain	Residue	Details
A	LYS51
A	TYR295

---

site_id	CSA2
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 15491139, 16524684

Chain	Residue	Details
A	TYR269

---

site_id	MCSA1
Number of Residues	3
Details	M-CSA 545

Chain	Residue	Details
A	LYS51	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
A	TYR269	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
A	TYR295	electrostatic stabiliser, proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	3
Details	M-CSA 545

Chain	Residue	Details
B	LYS51	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
B	TYR269	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
B	TYR295	electrostatic stabiliser, proton acceptor, proton donor

---

site_id	MCSA3
Number of Residues	3
Details	M-CSA 545

Chain	Residue	Details
C	LYS51	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
C	TYR269	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
C	TYR295	electrostatic stabiliser, proton acceptor, proton donor

---

site_id	MCSA4
Number of Residues	3
Details	M-CSA 545

Chain	Residue	Details
D	LYS51	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
D	TYR269	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
D	TYR295	electrostatic stabiliser, proton acceptor, proton donor

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