Structure of PDB 5i5m Chain B

Receptor sequence
>5i5mB (length=576) Species: 318161 (Shewanella denitrificans OS217) [Search protein sequence]
ASAVVHPGELDEYYGFWSGGHSGEVRILGIPSMRELMRIPVFNIDSATGW
GITNESKRIKGDSAHLMTGDSHHPHMSMTDGSYNGKYVFINDKANSRVAR
IRCDVMKTDKMITIPNVQAIHGLRVQKVPYTKYVICNGEFEIPMNNDGKA
SLEDVSTYRSLFNVIDAEKMEVAFQVMVDGNLDNTDADYDGKYFFSTCYN
SEMGMNLGEMITAERDHVVVFSLERCLAALKAGKFTNYNGNKVPVLDGRK
GSDLTRYIPVPKSPHGINTAPDGKYFVANGKLSPTVSVVEIARLDDVFSG
KIQPRDAIVAEPELGLGPLHTAFDNKGNAFTTLFLDSQIAKWNIQDAIKA
YNGEKVNYLRQKLDVHYQPGHNHTSQGETRDTDGKWLVVLCKFSKDRFLP
VGPLRPENDQLIDISGDEMKLVHDGPTFAEPHDCMIVHRSKVKPQKLWTR
DDPMFADTVAMAKQDGVTLEMDNKVIRDGNKVRVYMTSIAPNFGMNEFKV
KLGDEVTVVVTNLDQVEDVTHGFCMTNHGVQMEVAPQATASVTFIANKPG
VQWYYCNWFCHALHMEMRGRMLVEAL
3D structure
PDB5i5m Role of Calcium in Secondary Structure Stabilization during Maturation of Nitrous Oxide Reductase.
ChainB
Resolution1.37 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I542 P544
Catalytic site (residue number reindexed from 1) I489 P491
Enzyme Commision number 1.7.2.4: nitrous-oxide reductase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA B Y252 E255 M263 D269 S316 Y199 E202 M210 D216 S263
BS02 BU3 B S130 E221 S77 E168
Gene Ontology
Molecular Function
GO:0004129 cytochrome-c oxidase activity
GO:0005507 copper ion binding
GO:0005509 calcium ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0050304 nitrous-oxide reductase activity
Biological Process
GO:0019333 denitrification pathway
GO:1902600 proton transmembrane transport
Cellular Component
GO:0016020 membrane
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5i5m, PDBe:5i5m, PDBj:5i5m
PDBsum5i5m
PubMed26885878
UniProtQ12M27

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