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7THG

Crystal Structure Of Human NADH-Cytochrome B5 Reductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004128molecular_functioncytochrome-b5 reductase activity, acting on NAD(P)H
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005811cellular_componentlipid droplet
A0005833cellular_componenthemoglobin complex
A0006695biological_processcholesterol biosynthetic process
A0006809biological_processnitric oxide biosynthetic process
A0008015biological_processblood circulation
A0016020cellular_componentmembrane
A0016208molecular_functionAMP binding
A0016491molecular_functionoxidoreductase activity
A0031966cellular_componentmitochondrial membrane
A0035578cellular_componentazurophil granule lumen
A0043531molecular_functionADP binding
A0050421molecular_functionnitrite reductase (NO-forming) activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0051287molecular_functionNAD binding
A0071949molecular_functionFAD binding
A1903958cellular_componentnitric-oxide synthase complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:15502298, ECO:0007744|PDB:1UMK
ChainResidueDetails
AARG91
APRO92
ATYR93
AVAL108
ALYS110
APHE113
ALYS125
AMET126
ASER127
ATHR184

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS41

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ATYR42

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DCN2
ChainResidueDetails
ALYS119

219869

PDB entries from 2024-05-15

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