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1V5H

Crystal Structure of Human Cytoglobin (Ferric Form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0004784molecular_functionsuperoxide dismutase activity
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0010764biological_processnegative regulation of fibroblast migration
A0015671biological_processoxygen transport
A0016491molecular_functionoxidoreductase activity
A0019395biological_processfatty acid oxidation
A0019430biological_processremoval of superoxide radicals
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0032966biological_processnegative regulation of collagen biosynthetic process
A0043005cellular_componentneuron projection
A0043025cellular_componentneuronal cell body
A0046210biological_processnitric oxide catabolic process
A0046872molecular_functionmetal ion binding
A0047888molecular_functionfatty acid peroxidase activity
A0070025molecular_functioncarbon monoxide binding
A0098809molecular_functionnitrite reductase activity
A0141118molecular_functionnitric oxide dioxygenase activity, heme protein as donor
A2000490biological_processnegative regulation of hepatic stellate cell activation
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 191
ChainResidue
ASER55
ALEU89
AHIS113
ALYS116
AHIS117
AVAL119
ATYR123
APHE124
AHOH201
AHOH210
AALA56
ATYR59
APHE60
AGLN77
AHIS81
AARG84
AVAL85
AALA88

219140

PDB entries from 2024-05-01

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