3RGP: Catalase

Structural and Kinetic Analysis of the Beef liver Catalase complexed with Nitric Oxide. Determined by X-ray diffraction at 1.88 Å resolution. Released 11 May 2011.

Method: X-ray diffraction
Resolution: 1.88 Å
Organism: Bos taurus
Chains: 4
Atoms: 18,276
Mol. weight: 230.1 kDa
Ligands: HEM, NO
Released: 11 May 2011

Explore 3RGP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3RGP contains 118 α-helices and 92 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 30 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	10-17	8
α-helix	21-24	4
β-strand	25	1	1
α-helix	26	1
β-strand	27	1	2
α-helix	32	1
β-strand	33	1	2
α-helix	34	1
β-strand	41-43	3	3
α-helix	48	1
β-strand	49	1	3
β-strand	50	1	4
α-helix	54-63	10
α-helix	69-71	3
β-strand	77-86	10	5
α-helix	97-99	3
β-strand	105-113	9	5
β-strand	130-137	8	5
β-strand	140-147	8	5
α-helix	157-159	3
α-helix	160-167	8
β-strand	169	1	6
β-strand	176	1	6
α-helix	178-187	10
α-helix	189-191	3
α-helix	192-198	7
α-helix	201-203	3
β-strand	205	1	7
β-strand	213-214	2	5
β-strand	219-222	4	5
β-strand	228-237	10	5
β-strand	243	1	7
α-helix	246-255	10
α-helix	259-269	11
β-strand	275-283	9	5
α-helix	285-290	6
β-strand	310-319	10	5
α-helix	324	1
α-helix	325-329	5
β-strand	342-344	3	5
α-helix	348-364	17
α-helix	369-371	3
α-helix	373-375	3
β-strand	412	1	8
α-helix	415-417	3
α-helix	418-421	4
β-strand	423-427	5	9
β-strand	428-429	2	10
α-helix	440-444	5
α-helix	445-449	5
α-helix	452-466	15
α-helix	471-484	14
α-helix	486-499	14

Chain B: 28 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	10-16	7
α-helix	21-24	4
β-strand	25	1	11
α-helix	26	1
β-strand	27	1	12
β-strand	33	1	12
β-strand	41-43	3	13
α-helix	48	1
β-strand	49	1	13
β-strand	50	1	4
α-helix	54-63	10
α-helix	69-71	3
β-strand	77-86	10	14
α-helix	97-99	3
β-strand	105-113	9	14
β-strand	130-137	8	14
β-strand	140-147	8	14
α-helix	157-159	3
α-helix	160-167	8
β-strand	169	1	15
β-strand	176	1	15
α-helix	178-187	10
α-helix	189-191	3
α-helix	192-198	7
α-helix	201-203	3
β-strand	205	1	16
β-strand	213-214	2	14
β-strand	219-222	4	14
β-strand	228-237	10	14
β-strand	243	1	16
α-helix	246-255	10
α-helix	259-269	11
β-strand	275-283	9	14
α-helix	285-290	6
β-strand	310-319	10	14
α-helix	324	1
α-helix	325-329	5
β-strand	342-344	3	14
α-helix	348-364	17
α-helix	369-371	3
α-helix	373-375	3
β-strand	412	1	17
α-helix	415-417	3
α-helix	418-420	3
β-strand	423-427	5	9
β-strand	428-430	3	18
α-helix	440-444	5
α-helix	445-449	5
α-helix	452-466	15
α-helix	471-484	14
α-helix	486-499	14

Chain C: 30 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	10-16	7
α-helix	22-24	3
β-strand	25	1	8
α-helix	26	1
β-strand	27	1	19
α-helix	32	1
β-strand	33	1	19
α-helix	34	1
β-strand	41-43	3	18
α-helix	48	1
β-strand	49	1	18
β-strand	50	1	20
α-helix	54-63	10
α-helix	69-71	3
β-strand	77-86	10	21
α-helix	97-99	3
β-strand	105-113	9	21
β-strand	130-137	8	21
β-strand	140-147	8	21
α-helix	157-159	3
α-helix	160-167	8
β-strand	169	1	22
β-strand	176	1	22
α-helix	178-187	10
α-helix	189-191	3
α-helix	192-198	7
α-helix	201-203	3
β-strand	205	1	23
β-strand	213-214	2	21
β-strand	219-222	4	21
β-strand	228-237	10	21
β-strand	243	1	23
α-helix	246-255	10
α-helix	259-269	11
β-strand	275-283	9	21
α-helix	285-290	6
β-strand	310-319	10	21
α-helix	324	1
α-helix	325-329	5
β-strand	342-344	3	21
α-helix	348-364	17
α-helix	369-371	3
α-helix	373-375	3
β-strand	412	1	1
α-helix	415-417	3
α-helix	418-421	4
β-strand	422-424	3	3
β-strand	427-430	4	13
α-helix	440-444	5
α-helix	445-449	5
α-helix	452-466	15
α-helix	471-484	14
α-helix	486-499	14

Chain D: 30 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	10-17	8
α-helix	21-24	4
β-strand	25	1	17
α-helix	26	1
β-strand	27	1	24
α-helix	32	1
β-strand	33	1	24
α-helix	34	1
β-strand	42-43	2	10
α-helix	48	1
β-strand	49	1	10
β-strand	50	1	20
α-helix	54-63	10
α-helix	69-71	3
β-strand	77-86	10	25
α-helix	97-99	3
β-strand	105-113	9	25
β-strand	130-137	8	25
β-strand	140-147	8	25
α-helix	157-159	3
α-helix	160-167	8
β-strand	169	1	26
β-strand	176	1	26
α-helix	178-187	10
α-helix	189-191	3
α-helix	192-198	7
α-helix	201-203	3
β-strand	205	1	27
β-strand	213-214	2	25
β-strand	219-222	4	25
β-strand	228-237	10	25
β-strand	243	1	27
α-helix	246-255	10
α-helix	259-269	11
β-strand	275-283	9	25
α-helix	285-288	4
β-strand	310-319	10	25
α-helix	324	1
α-helix	325-329	5
β-strand	342-344	3	25
α-helix	348-364	17
α-helix	369-371	3
α-helix	373-375	3
β-strand	412	1	11
α-helix	415-417	3
α-helix	418-421	4
β-strand	422-423	2	13
β-strand	426-430	5	3
α-helix	440-444	5
α-helix	445-449	5
α-helix	452-466	15
α-helix	471-484	14
α-helix	486-499	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Catalase	A, B, C, D	protein	499	Bos taurus	P00432 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>3RGP_1 Catalase (chains A, B, C, D)
NRDPASDQMKHWKEQRAAQKPDVLTTGGGNPVGDKLNSLTVGPRGPLLVQDVVFTDEMAH
FDRERIPERVVHAKGAGAFGYFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSA
DTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDALLFPSFIHSQKRNPQTHLKDPDMVW
DFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIK
NLSVEDAARLAHEDPDYGLRDLFNAIATGNYPSWTLYIQVMTFSEAEIFPFNPFDLTKVW
PHGDYPLIPVGKLVLNRNPVNYFAEVEQLAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHR
HRLGPNYLQIPVNCPYRARVANYQRDGPMCMMDNQGGAPNYYPNSFSAPEHQPSALEHRT
HFSGDVQRFNSANDDNVTQVRTFYLKVLNEEQRKRLCENIAGHLKDAQLFIQKKAVKNFS
DVHPEYGSRIQALLDKYNE

Ligands and cofactors

ID	Name	Formula	Copies
HEM	Protoporphyrin IX containing FE	C34 H32 Fe N4 O4	4
NO	Nitric oxide	N O	4

Primary citation

Interaction of nitric oxide with catalase: structural and kinetic analysis. Purwar, N., McGarry, J.M., Kostera, J. et al. Biochemistry (2011) 50:4491-4503. DOI 10.1021/bi200130r · PubMed

Other PDB entries of the same protein (UniProt P00432 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6PO0 1.75 Å, The structure of the orthorhombic (P212121) crystal form of beef liver catalase at 1.85…
6PM7 1.85 Å, The structure of the triclinic crystal form of beef liver catalase at 1.85 A resolution
3RE8 1.9 Å, Structural and Kinetic Analysis of the Beef liver Catalase interacting with Nitric Oxide
3RGS 1.99 Å, Structural and kinetic analysis of the beef liver catalase with the ammonia as a ligand
4BLC 2.3 Å, The structure of orthorhombic crystals of beef liver catalase
7CAT 2.5 Å, The NADPH binding site on beef liver catalase
8CAT 2.5 Å, The NADPH binding site on beef liver catalase
3NWL 2.69 Å, The crystal structure of the P212121 form of bovine liver catalase previously…
1TGU 2.8 Å, The crystal structure of bovine liver catalase without NADPH
1TH2 2.8 Å, crystal structure of NADPH depleted bovine liver catalase complexed with azide
1TH3 2.8 Å, Crystal structure of NADPH depleted bovine live catalase complexed with cyanide
1TH4 2.98 Å, crystal structure of NADPH depleted bovine liver catalase complexed with…

Browse structure collections

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