1Q4G: Prostaglandin G/H synthase 1

2.0 Angstrom Crystal Structure of Ovine Prostaglandin H2 Synthase-1, in complex with alpha-methyl-4-biphenylacetic acid. Determined by X-ray diffraction at 2.0 Å resolution. Released 6 Jan 2004.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Ovis aries
Chains
2
Atoms
10,336
Mol. weight
136.1 kDa
Ligands
HEM, BFL, BOG
Released
6 Jan 2004

Explore 1Q4G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Q4G contains 94 α-helices and 62 β-strands across 2 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: 46 helices, 31 β-strands

ElementResiduesLengthSheet
α-helix35-384
β-strand46-5051
β-strand54-5851
β-strand64-6522
β-strand71-7222
α-helix74-829
α-helix83-853
α-helix86-938
α-helix97-1037
α-helix108-12114
β-strand130-13123
α-helix139-1435
β-strand14714
β-strand149-15023
α-helix153-1564
β-strand16115
β-strand16415
α-helix171-1733
α-helix174-1774
α-helix178-1825
β-strand18316
β-strand18917
β-strand19418
β-strand19519
α-helix196-20611
β-strand212110
β-strand22014
β-strand221110
α-helix231-2344
α-helix238-2447
β-strand245111
α-helix2511
β-strand252111
α-helix2531
β-strand255-257312
β-strand260-262312
α-helix263-2642
β-strand265113
α-helix281-2833
β-strand285113
α-helix292-2943
α-helix296-31924
α-helix325-34319
α-helix344-3485
α-helix349-3535
α-helix363-3664
β-strand37813
α-helix379-3846
α-helix388-3903
β-strand395-397314
β-strand400-402314
α-helix404-4074
α-helix413-4175
α-helix419-42810
β-strand43019
α-helix4311
β-strand43217
α-helix4331
β-strand44016
α-helix445-45713
α-helix460-4623
α-helix463-4697
α-helix473-4753
α-helix478-4825
α-helix486-49510
α-helix498-5003
α-helix503-5097
α-helix5111
β-strand512115
α-helix5131
β-strand519115
α-helix520-53516
α-helix538-5403
α-helix547-5504
α-helix553-5608
α-helix564-5696
β-strand58118
Chain B: 48 helices, 31 β-strands
ElementResiduesLengthSheet
α-helix35-384
β-strand46-50516
β-strand54-58516
β-strand64-65217
β-strand71-72217
α-helix74-829
α-helix83-853
α-helix86-938
α-helix97-1048
α-helix108-12114
β-strand130-131218
α-helix139-1435
β-strand147119
β-strand149-150218
α-helix153-1564
β-strand161120
β-strand164120
α-helix171-1733
α-helix174-1818
β-strand183121
β-strand189122
β-strand194123
β-strand195124
α-helix196-20611
β-strand212125
β-strand220119
β-strand221125
α-helix231-2344
α-helix238-2447
β-strand245126
α-helix2511
β-strand252126
α-helix2531
β-strand255-257327
β-strand260-262327
α-helix263-2642
β-strand265128
α-helix281-2833
α-helix2841
β-strand285128
α-helix2861
α-helix292-2943
α-helix296-31924
α-helix325-34319
α-helix344-3485
α-helix349-3535
α-helix363-3664
β-strand378118
α-helix379-3846
α-helix388-3903
β-strand395-397329
β-strand400-402329
α-helix404-4074
α-helix413-4175
α-helix419-42810
β-strand430124
α-helix4311
β-strand432122
α-helix4331
β-strand440121
α-helix442-4443
α-helix445-45713
α-helix460-4623
α-helix463-4697
α-helix473-4753
α-helix478-4825
α-helix486-49510
α-helix498-5003
α-helix503-5097
α-helix5111
β-strand512130
α-helix5131
β-strand519130
α-helix520-53516
α-helix538-5403
α-helix547-5504
α-helix553-5608
α-helix564-5696
β-strand581123

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Prostaglandin G/H synthase 1A, Bprotein553Ovis ariesP05979 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1Q4G_1 Prostaglandin G/H synthase 1 (chains A, B)
PVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPEIWTWLRTTLRPSPSFIHF
LLTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTYNIAHDYISWESFSNVSYYTRI
LPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFK
TSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPV
LMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHNRVCDLLKAEHPTWGDEQLFQT
ARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLM
PDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNIDHHILHVAVDV
IKESRVLRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEK
CHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGEVGFNLVKTATLKKLVCLN
TKTCPYVSFHVPD

Ligands and cofactors

IDNameFormulaCopies
HEMProtoporphyrin IX containing FEC34 H32 Fe N4 O42
BFL2-(1,1'-biphenyl-4-yl)propanoic acidC15 H14 O22
BOGoctyl beta-D-glucopyranosideC14 H28 O68

Water and common crystallization additives (GOL) are not listed.

Primary citation

The 2.0A Resolution Crystal Structure of Prostaglandin H(2) Synthase-1: Structural Insights into an Unusual Peroxidase. Gupta, K., Selinsky, B.S., Kaub, C.J. et al. J Mol Biol (2004) 335:503-518. DOI 10.1016/j.jmb.2003.10.073 · PubMed

Other PDB entries of the same protein (UniProt P05979 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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