1N7M: Germline 7G12 with N-methylmesoporphyrin

Germline 7G12 with N-methylmesoporphyrin. Determined by X-ray diffraction at 1.8 Å resolution. Released 4 Feb 2003.

Method
X-ray diffraction
Resolution
1.8 Å
Organisms
Mus musculus, Homo sapiens
Chains
2
Atoms
3,809
Mol. weight
46.98 kDa
Ligands
MMP
Released
4 Feb 2003

Explore 1N7M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1N7M contains 16 α-helices and 43 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 H: 8 helices, 21 β-strands

ElementResiduesLengthSheet
β-strand4-741
β-strand10-1342
β-strand19-2571
β-strand33-3862
β-strand45-4952
β-strand53-5422
α-helix551
β-strand62-6761
β-strand70-7561
α-helix80-823
β-strand85-9062
α-helix961
β-strand97-9822
β-strand102-10652
β-strand11113
α-helix112-1132
β-strand114-11854
α-helix121-1255
β-strand129-139114
β-strand14013
β-strand145-15065
β-strand153-15425
α-helix1551
β-strand159-16354
α-helix164-1674
β-strand173-182104
α-helix183-1886
β-strand191-19775
β-strand205-21065
Chain L: 8 helices, 22 β-strands
ElementResiduesLengthSheet
β-strand3-646
β-strand9-1242
β-strand18-2586
α-helix29-313
β-strand34-4072
β-strand44-5182
β-strand58-6032
α-helix62-643
β-strand68-7366
β-strand78-8366
α-helix88-903
β-strand92-9872
β-strand10412
β-strand108-11252
β-strand11817
α-helix119-1202
β-strand121-12558
α-helix126-1283
β-strand136-146118
β-strand14717
β-strand152-15549
α-helix156-1583
β-strand16019
β-strand164-16638
α-helix167-1693
β-strand170-17128
β-strand177-186108
β-strand196-20169
α-helix202-2043
β-strand206-21169

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Germline Metal Chelatase Catalytic Antibody, chain HHprotein213Mus musculus, Homo sapiens
Germline Metal Chelatase Catalytic Antibody, chain LLprotein216Mus musculus, Homo sapiensP01857 (AlphaFold model)
Sequence of entity 1 (H), FASTA
>1N7M_1 Germline Metal Chelatase Catalytic Antibody, chain H (chains H)
ELVMTQTPKFMSTSVGDRVSITCKASQNVGTAVAWYQQKPGQSPKLLIYSASNRYTGVPD
RFTGSGSGTDFTLTISNMQSEDLADYFCQQYSSYPLTFGGGTKVEIKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGE
Sequence of entity 2 (L), FASTA
>1N7M_2 Germline Metal Chelatase Catalytic Antibody, chain L (chains L)
QVQLLESGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNSGGTKY
NEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCTRRDSDYWGAGTTVTVSSASTKGP
SVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLS
SVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKS

Ligands and cofactors

IDNameFormulaCopies
MMPN-methylmesoporphyrinC35 H40 N4 O41

Primary citation

Structural evidence for substrate strain in antibody catalysis. Yin, J., Andryski, S.E., Beuscher IV, A.E. et al. Proc Natl Acad Sci U S A (2003) 100:856-861. DOI 10.1073/pnas.0235873100 · PubMed

Other PDB entries of the same protein (UniProt P01857 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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