3KOW

Crystal Structure of ornithine 4,5 aminomutase backsoaked complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0016853	molecular_function	isomerase activity
A	0031419	molecular_function	cobalamin binding
A	0046872	molecular_function	metal ion binding
A	0046983	molecular_function	protein dimerization activity
A	0047831	molecular_function	D-ornithine 4,5-aminomutase activity
B	0003824	molecular_function	catalytic activity
B	0016853	molecular_function	isomerase activity
B	0031419	molecular_function	cobalamin binding
B	0046872	molecular_function	metal ion binding
B	0046983	molecular_function	protein dimerization activity
B	0047831	molecular_function	D-ornithine 4,5-aminomutase activity
C	0003824	molecular_function	catalytic activity
C	0016853	molecular_function	isomerase activity
C	0031419	molecular_function	cobalamin binding
C	0046872	molecular_function	metal ion binding
C	0046983	molecular_function	protein dimerization activity
C	0047831	molecular_function	D-ornithine 4,5-aminomutase activity
D	0003824	molecular_function	catalytic activity
D	0016853	molecular_function	isomerase activity
D	0031419	molecular_function	cobalamin binding
D	0046872	molecular_function	metal ion binding
D	0046983	molecular_function	protein dimerization activity
D	0047831	molecular_function	D-ornithine 4,5-aminomutase activity
E	0003824	molecular_function	catalytic activity
E	0016853	molecular_function	isomerase activity
E	0031419	molecular_function	cobalamin binding
E	0047831	molecular_function	D-ornithine 4,5-aminomutase activity
F	0003824	molecular_function	catalytic activity
F	0016853	molecular_function	isomerase activity
F	0031419	molecular_function	cobalamin binding
F	0047831	molecular_function	D-ornithine 4,5-aminomutase activity
G	0003824	molecular_function	catalytic activity
G	0016853	molecular_function	isomerase activity
G	0031419	molecular_function	cobalamin binding
G	0047831	molecular_function	D-ornithine 4,5-aminomutase activity
H	0003824	molecular_function	catalytic activity
H	0016853	molecular_function	isomerase activity
H	0031419	molecular_function	cobalamin binding
H	0047831	molecular_function	D-ornithine 4,5-aminomutase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE B12 A 1801

Chain	Residue
A	ASP616
A	SER667
A	ILE669
A	ILE670
A	SER671
A	HIS672
A	GLY701
A	GLY702
A	THR703
A	PHE719
A	GLY720
A	GLU617
A	GLY722
A	SER723
A	VAL728
C	TYR116
C	ILE127
C	ASP493
C	5AD1500
A	HIS618
A	SER619
A	VAL620
A	GLY621
A	VAL625
A	LEU665
A	ALA666

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PLP C 1802

Chain	Residue
A	ARG109
A	GLY112
A	GLN113
A	SER114
A	TYR160
A	SER162
A	TYR187
A	ARG192
A	ASN226
C	LYS629

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE 5AD C 1500

Chain	Residue
A	B121801
C	LEU489

---

site_id	AC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE B12 D 1801

Chain	Residue
B	ALA111
B	HIS115
B	TYR116
B	ASP490
D	GLU615
D	GLU617
D	HIS618
D	SER619
D	VAL620
D	GLY621
D	VAL625
D	ALA666
D	SER667
D	ILE669
D	ILE670
D	SER671
D	HIS672
D	GLY701
D	GLY702
D	THR703
D	PHE719
D	GLY720
D	SER723
D	VAL728

---

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP B 1802

Chain	Residue
B	LYS629
D	ARG109
D	GLY112
D	GLN113
D	SER114
D	TYR160
D	SER162
D	HIS182
D	TYR187
D	ARG192
D	HIS225
D	ASN226

---

site_id	AC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE B12 C 1801

Chain	Residue
A	ALA111
A	TYR116
A	ASP490
A	5AD1500
C	GLU615
C	ASP616
C	GLU617
C	HIS618
C	SER619
C	VAL620
C	GLY621
C	LEU622
C	GLU624
C	VAL625
C	SER667
C	ILE670
C	SER671
C	HIS672
C	GLY701
C	GLY702
C	THR703
C	PHE719
C	GLY720
C	SER723
C	VAL728

---

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP A 1802

Chain	Residue
A	LYS629
C	ARG109
C	GLY112
C	GLN113
C	SER114
C	TYR160
C	SER162
C	HIS182
C	TYR187
C	ARG192
C	HIS225
C	ASN226

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 5AD A 1500

Chain	Residue
A	GLU121
A	LEU489
A	ASP490
C	B121801

---

site_id	AC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE B12 B 1801

Chain	Residue
B	GLU615
B	GLU617
B	HIS618
B	SER619
B	VAL620
B	GLY621
B	LEU622
B	VAL625
B	LEU665
B	SER667
B	ILE669
B	SER671
B	HIS672
B	GLY701
B	GLY702
B	THR703
B	PHE719
B	GLY720
B	SER723
B	VAL728
D	TYR116
D	ASP490
D	ASP493
D	5AD1500

---

site_id	BC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP D 1802

Chain	Residue
B	ARG109
B	GLY112
B	GLN113
B	SER114
B	TYR160
B	SER162
B	HIS182
B	TYR187
B	ARG192
B	HIS225
B	ASN226
D	LYS629

---

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 5AD D 1500

Chain	Residue
B	B121801
D	GLU121
D	LEU489

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20106986","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20106986","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"20106986","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---