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3GKT

Crystal structure of murine neuroglobin under Kr pressure

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0046872molecular_functionmetal ion binding
A0071456biological_processcellular response to hypoxia
A0098809molecular_functionnitrite reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 152
ChainResidue
ASER19
APRO20
ALEU21
AGLU22
AARG66

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE KR A 154
ChainResidue
ALEU56
AHOH226
APHE28
AALA29
APHE32
ASER55

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 155
ChainResidue
ALEU38
ALEU41
APHE42
ATYR44
AHIS64
ALYS67
ALYS67
AVAL68
AVAL71
ATYR88
ALEU92
ALYS95
AHIS96
AVAL101
APHE106
AVAL109
AHOH173
AHOH176
AHOH176
AHOH197

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
AHIS64

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
AHIS96

227111

PDB entries from 2024-11-06

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