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2HZ2

The x-ray crystal structure of ferric Synechocystis hemoglobin H117A mutant with a covalent linkage

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005737cellular_componentcytoplasm
A0008379molecular_functionthioredoxin peroxidase activity
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
A0045454biological_processcell redox homeostasis
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 201
ChainResidue
AASP15
AASP19
AHIS33
AHIS77

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 202
ChainResidue
AGLU72
AASP120
AHOH206
AHOH249
AHOH329

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 203
ChainResidue
ASER2
AGLU6
AHOH274
AHOH276
AHOH296

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 204
ChainResidue
ALYS32
AHIS33
AARG44
ALYS48
AHOH205
AHOH222

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM A 125
ChainResidue
APHE34
AVAL38
ALYS42
AHIS46
APHE50
ATYR53
ATYR65
AMET66
AHIS70
ALEU73
APHE84
AVAL87
AGLY99
AHOH228
AHOH233
AHOH314

Functional Information from PROSITE/UniProt
site_idPS01213
Number of Residues21
DetailsGLOBIN_FAM_2 Protozoan/cyanobacterial globins signature. FLtyafGGTdkYdGRy....MreaH
ChainResidueDetails
APHE50-HIS70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: distal binding residue
ChainResidueDetails
AHIS46

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue
ChainResidueDetails
AHIS70

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: covalent
ChainResidueDetails
AALA117

223532

PDB entries from 2024-08-07

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