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1GVH

The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unespected geometry of the distal heme pocket

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005504molecular_functionfatty acid binding
A0005737cellular_componentcytoplasm
A0008941molecular_functionnitric oxide dioxygenase NAD(P)H activity
A0009636biological_processresponse to toxic substance
A0015671biological_processoxygen transport
A0016491molecular_functionoxidoreductase activity
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0032843molecular_functionhydroperoxide reductase activity
A0046210biological_processnitric oxide catabolic process
A0046872molecular_functionmetal ion binding
A0051409biological_processresponse to nitrosative stress
A0071500biological_processcellular response to nitrosative stress
A0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A1399
ChainResidue
ALYS40
APHE43
AGLN201
AGLU202

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A1400
ChainResidue
AGLN271
AHIS294
AHIS302
AALA303
AHOH2137

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A1401
ChainResidue
AGLY51

site_idAC4
Number of Residues27
DetailsBINDING SITE FOR RESIDUE FAD A1397
ChainResidue
AASN44
ASER46
AGLN48
AASN50
ATYR188
AARG204
AGLN205
ATYR206
ASER207
AALA220
AVAL221
ALYS222
AGLU224
AGLU225
AGLY227
AGLN228
AVAL229
ASER230
AVAL269
ATHR272
AGLU388
APHE390
AHOH2095
AHOH2103
AHOH2187
AHOH2188
AHOH2189

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A1398
ChainResidue
ALEU39
AASN44
AGLN53
AALA56
ALEU57
AALA60
AILE61
AILE81
ALYS84
AHIS85
APHE88
AILE90
AGLN94
ATYR95
AVAL98
ALEU127
APRO392
AHIS393
AHOH2190
AHOH2191

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:11092893
ChainResidueDetails
ATYR95
AGLU135

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue
ChainResidueDetails
AHIS85

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ATYR188
AARG204
ACYS389

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY268

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Involved in heme-bound ligand stabilization and O-O bond activation
ChainResidueDetails
ATYR29

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Influences the redox potential of the prosthetic heme and FAD groups
ChainResidueDetails
ALYS84
AGLU388

220113

PDB entries from 2024-05-22

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