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6RA6

Ferric murine neuroglobin Gly-loop44-47/F106A mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0005092molecular_functionGDP-dissociation inhibitor activity
A0005344molecular_functionoxygen carrier activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0015671biological_processoxygen transport
A0016491molecular_functionoxidoreductase activity
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0031175biological_processneuron projection development
A0043066biological_processnegative regulation of apoptotic process
A0043204cellular_componentperikaryon
A0046872molecular_functionmetal ion binding
A0070301biological_processcellular response to hydrogen peroxide
A0071456biological_processcellular response to hypoxia
A0098809molecular_functionnitrite reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue HEM A 201
ChainResidue
ALEU31
ALEU91
ALYS94
AHIS95
AVAL98
AVAL100
AVAL108
AHOH309
AHOH329
ALEU38
ALEU41
APHE42
APRO58
AHIS63
AVAL67
AVAL70
ATYR87

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 202
ChainResidue
AARG3
AARG10
AARG18

site_idAC3
Number of Residues6
Detailsbinding site for residue TRS A 203
ChainResidue
ATRP13
ASER17
APRO20
AARG65
AASP72
AHOH312

site_idAC4
Number of Residues2
Detailsbinding site for residue PEG A 204
ChainResidue
ATYR87
AHOH311

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL A 205
ChainResidue
AHIS0
AVAL78
AHOH306

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL A 206
ChainResidue
AARG30
AALA33
ATYR114
ATYR114
ALYS118

site_idAC7
Number of Residues5
Detailsbinding site for residue PEG A 207
ChainResidue
AARG30
ATYR114
ATYR114
ALYS118
ALYS118

site_idAC8
Number of Residues3
Detailsbinding site for residue PEG A 208
ChainResidue
AARG101
ALEU102
ASER103

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: distal binding residue; reversible => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:15162488, ECO:0007744|PDB:1Q1F
ChainResidueDetails
AHIS63

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:15162488, ECO:0000269|PubMed:15548613, ECO:0007744|PDB:1Q1F, ECO:0007744|PDB:1W92
ChainResidueDetails
AHIS95

219869

PDB entries from 2024-05-15

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