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4B3W

Crystal structure of human cytoglobin H(E7)Q mutant

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
B0001666biological_processresponse to hypoxia
B0004096molecular_functioncatalase activity
B0004601molecular_functionperoxidase activity
B0004784molecular_functionsuperoxide dismutase activity
B0005344molecular_functionoxygen carrier activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006979biological_processresponse to oxidative stress
B0010764biological_processnegative regulation of fibroblast migration
B0015671biological_processoxygen transport
B0016491molecular_functionoxidoreductase activity
B0019395biological_processfatty acid oxidation
B0019430biological_processremoval of superoxide radicals
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0032966biological_processnegative regulation of collagen biosynthetic process
B0043005cellular_componentneuron projection
B0043025cellular_componentneuronal cell body
B0046210biological_processnitric oxide catabolic process
B0046872molecular_functionmetal ion binding
B0047888molecular_functionfatty acid peroxidase activity
B0070025molecular_functioncarbon monoxide binding
B0098809molecular_functionnitrite reductase activity
B0141118molecular_functionnitric oxide dioxygenase activity, heme protein as donor
B2000490biological_processnegative regulation of hepatic stellate cell activation
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM A 200
ChainResidue
APHE49
ATYR123
APHE124
ALEU127
ACYN300
AHOH2011
ATYR59
APHE60
AGLN81
AARG84
ALEU89
AHIS113
AHIS117
AVAL119

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CYN A 300
ChainResidue
AGLN81
AVAL85
AHEM200

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FC6 A 400
ChainResidue
ALYS125
AARG155
AGLY156
ATYR159
BPRO54
BSER55

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM B 200
ChainResidue
AGLU137
AGLU138
AALA140
ASER141
BTYR59
BPHE60
BGLN62
BGLN81
BARG84
BALA88
BHIS113
BHIS117
BVAL119
BTYR123
BPHE124
BCYN300

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CYN B 300
ChainResidue
BGLN81
BVAL85
BHEM200

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FC6 B 400
ChainResidue
APHE53
APRO54
ASER55
BLYS125
BARG155
BGLY156
BTYR159

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT B 1172
ChainResidue
BGLN77

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PDB entries from 2024-06-12

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