3E7G: Human INOSOX with inhibitor AR-C95791

Structure of human INOSOX with inhibitor AR-C95791. Determined by X-ray diffraction at 2.2 Å resolution. Released 7 Oct 2008.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 4
Atoms: 14,516
Mol. weight: 200.81 kDa
Ligands: HEM, H4B, AT2, ZN
Released: 7 Oct 2008

Explore 3E7G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3E7G contains 116 α-helices and 108 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, 27 β-strands

Element	Residues	Length	Sheet
β-strand	85-88	4	1
β-strand	89	1	2
β-strand	95-98	4	1
α-helix	100-103	4
β-strand	115	1	3
α-helix	123-125	3
β-strand	126	1	4
α-helix	133-135	3
α-helix	136-152	17
α-helix	159-175	17
α-helix	183-195	13
α-helix	203-205	3
β-strand	210-213	4	5
α-helix	220-235	16
α-helix	236-238	3
β-strand	243-246	4	5
α-helix	248-250	3
β-strand	258-259	2	6
β-strand	263	1	5
β-strand	267	1	7
β-strand	269-271	3	8
β-strand	277-279	3	8
α-helix	281-283	3
α-helix	284-292	9
α-helix	295-297	3
α-helix	303	1
β-strand	304	1	7
α-helix	305-306	2
β-strand	307-310	4	6
α-helix	314-316	3
β-strand	317-319	3	6
α-helix	320-322	3
α-helix	323-325	3
β-strand	328-330	3	9
α-helix	337-342	6
β-strand	345-347	3	9
β-strand	351-352	2	5
β-strand	356-359	4	10
β-strand	362-364	3	10
β-strand	369-370	2	5
β-strand	374	1	11
α-helix	375-376	2
α-helix	377-382	6
α-helix	383-384	2
α-helix	392-399	8
α-helix	406-408	3
α-helix	410-428	19
β-strand	434	1	11
α-helix	436-454	19
α-helix	461-464	4
α-helix	470-472	3
α-helix	474-477	4
β-strand	478	1	2
β-strand	482	1	12
β-strand	488-490	3	10
β-strand	491	1	4
α-helix	495-498	4

Chain B: 29 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	85-88	4	13
β-strand	89	1	14
β-strand	95-98	4	13
α-helix	100-103	4
β-strand	115	1	12
α-helix	123-125	3
β-strand	126	1	15
α-helix	133-135	3
α-helix	136-152	17
α-helix	159-176	18
α-helix	183-195	13
α-helix	203-205	3
β-strand	210-213	4	16
α-helix	220-235	16
α-helix	236-238	3
β-strand	243-246	4	16
α-helix	248-250	3
β-strand	258-259	2	17
β-strand	263	1	16
β-strand	267	1	18
β-strand	269-271	3	19
β-strand	277-279	3	19
α-helix	281-283	3
α-helix	284-292	9
α-helix	303	1
β-strand	304	1	18
α-helix	305-306	2
β-strand	307-310	4	17
α-helix	314-316	3
β-strand	317-319	3	17
α-helix	320-322	3
α-helix	323-325	3
β-strand	328-330	3	20
α-helix	337-342	6
β-strand	345-347	3	20
β-strand	351-352	2	16
β-strand	356-359	4	21
β-strand	362-364	3	21
β-strand	369-370	2	16
β-strand	374	1	22
α-helix	375-376	2
α-helix	377-382	6
α-helix	383-384	2
α-helix	392-399	8
α-helix	406-408	3
α-helix	410-428	19
β-strand	434	1	22
α-helix	436-454	19
α-helix	461-464	4
α-helix	470-472	3
α-helix	474-477	4
β-strand	478	1	14
β-strand	482	1	3
β-strand	488-490	3	21
β-strand	491	1	15
α-helix	495-498	4

Chain C: 29 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	85-88	4	23
β-strand	89	1	24
β-strand	95-98	4	23
α-helix	100-103	4
β-strand	115	1	25
α-helix	123-125	3
β-strand	126	1	26
α-helix	133-135	3
α-helix	136-151	16
α-helix	159-176	18
α-helix	183-195	13
α-helix	203-205	3
β-strand	210-213	4	27
α-helix	220-235	16
α-helix	236-238	3
β-strand	243-246	4	27
α-helix	248-250	3
β-strand	258-259	2	28
β-strand	263	1	27
β-strand	267	1	29
β-strand	269-271	3	30
β-strand	277-279	3	30
α-helix	281-283	3
α-helix	284-292	9
α-helix	303	1
β-strand	304	1	29
α-helix	305-306	2
β-strand	307-310	4	28
α-helix	314-316	3
β-strand	317-319	3	28
α-helix	320-322	3
α-helix	323-325	3
β-strand	328-330	3	31
α-helix	337-342	6
β-strand	345-347	3	31
β-strand	351-352	2	27
β-strand	356-359	4	32
β-strand	362-364	3	32
β-strand	369-370	2	27
β-strand	374	1	33
α-helix	375-376	2
α-helix	377-382	6
α-helix	383-384	2
α-helix	392-398	7
α-helix	406-408	3
α-helix	410-428	19
β-strand	434	1	33
α-helix	436-454	19
α-helix	461-464	4
α-helix	470-472	3
α-helix	474-477	4
β-strand	478	1	24
β-strand	482	1	34
β-strand	488-490	3	32
β-strand	491	1	26
α-helix	495-497	3

Chain D: 28 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	85-88	4	35
β-strand	89	1	36
β-strand	95-98	4	35
α-helix	100-102	3
β-strand	115	1	34
α-helix	123-125	3
β-strand	126	1	37
α-helix	133-135	3
α-helix	136-151	16
α-helix	159-176	18
α-helix	183-195	13
α-helix	203-205	3
β-strand	210-213	4	38
α-helix	220-235	16
α-helix	236-238	3
β-strand	243-246	4	38
α-helix	248-250	3
β-strand	258-259	2	39
β-strand	263	1	38
β-strand	267	1	40
β-strand	269-271	3	41
β-strand	277-279	3	41
α-helix	281-283	3
α-helix	284-292	9
α-helix	303	1
β-strand	304	1	40
α-helix	305-306	2
β-strand	307-310	4	39
β-strand	317-319	3	39
α-helix	320-322	3
α-helix	323-325	3
β-strand	328-330	3	42
α-helix	337-342	6
β-strand	345-347	3	42
β-strand	351-352	2	38
β-strand	356-359	4	43
β-strand	362-364	3	43
β-strand	369-370	2	38
β-strand	374	1	44
α-helix	375-376	2
α-helix	377-382	6
α-helix	383-384	2
α-helix	392-398	7
α-helix	406-408	3
α-helix	410-428	19
β-strand	434	1	44
α-helix	436-454	19
α-helix	461-464	4
α-helix	470-472	3
α-helix	474-477	4
β-strand	478	1	36
β-strand	482	1	25
β-strand	488-490	3	43
β-strand	491	1	37
α-helix	495-497	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Nitric oxide synthase, inducible	A, B, C, D	protein	424	Homo sapiens	P35228 (AlphaFold model)

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

>3E7G_1 Nitric oxide synthase, inducible (chains A, B, C, D)
PRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDKPTPPDELLP
QAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCI
GRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNIRSAITVFPQRSDGKHDFRVWN
AQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYGRFDVVPLVLQANGRDPELFEI
PPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVR
DFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAE
SFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEMLNYVLSPFYYYQVEAWKTHVW
QDEK

Ligands and cofactors

ID	Name	Formula	Copies
HEM	Protoporphyrin IX containing FE	C34 H32 Fe N4 O4	4
H4B	5,6,7,8-tetrahydrobiopterin	C9 H15 N5 O3	4
AT2	Ethyl 4-[(4-methylpyridin-2-yl)amino]piperidine-1-carboxylate	C14 H21 N3 O2	4
ZN	Zinc ion	Zn	2

Primary citation

Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase. Garcin, E.D., Arvai, A.S., Rosenfeld, R.J. et al. Nat Chem Biol (2008) 4:700-707. DOI 10.1038/nchembio.115 · PubMed

Other PDB entries of the same protein (UniProt P35228 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6JWM 1.23 Å, Crystal structure of the SPRY domain of SPSB2 in complex with cR7, a potent cyclic…
6KEY 1.24 Å, Structural basis for the regulation of inducible nitric oxide synthase (iNOS) by the…
5XN3 1.34 Å, Crystal structure of SPSB2 in complex with a rational designed RGD containing cyclic…
6JWN 1.61 Å, Crystal structure of the SPRY domain of SPSB2 in complex with cR9, a cyclic peptide…
4NOS 2.25 Å, Human inducible nitric oxide synthase with inhibitor
3HR4 2.5 Å, Human iNOS Reductase and Calmodulin Complex
1NSI 2.55 Å, Human inducible nitric oxide synthase, ZN-bound, L-arg complex
3EJ8 2.55 Å, Structure of double mutant of human iNOS oxygenase domain with bound immidazole
2NSI 3.0 Å, Human inducible nitric oxide synthase, ZN-free, seitu complex
4CX7 3.16 Å, Structure of human iNOS heme domain in complex with (R)-6-(3-AMINO-2-(5-(2-(6-AMINO-4-…
2LL6 Solution NMR structure of CaM bound to iNOS CaM binding domain peptide
5TP6 Solution structure of the CaM34 with the iNOS CaM binding domain peptide

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