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1UMK

The Structure of Human Erythrocyte 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 PDB Data
site_idAC1
Number of Residues29
DetailsBINDING SITE FOR RESIDUE FAD A 1301
ChainResidue
AARG91
APHE120
AGLY123
AGLY124
ALYS125
AMET126
ASER127
ATHR181
ATHR184
AHOH1419
AHOH1422
APRO92
AHOH1438
AHOH1520
AHOH1708
AHOH1709
AHOH1710
AHOH1711
AHOH1790
AHOH1804
AHOH1805
AHOH2023
ATYR93
ATHR94
AVAL108
AILE109
ALYS110
ATYR112
APHE113

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:15502298, ECO:0007744|PDB:1UMK
ChainResidueDetails
APRO92
APRO185
ATYR93
ATHR94
AILE109
AVAL111
ALYS114
AMET126
ASER127
AGLN128

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ATYR42

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648
ChainResidueDetails
APRO43

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DCN2
ChainResidueDetails
APHE120

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndh
ChainResidueDetails
ATYR93

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PDB entries from 2024-07-24

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