Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2GL3

Crystal structure of Mycobacterium tuberculosis trHbN, TyrB10Phe GlnE11Val mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008379molecular_functionthioredoxin peroxidase activity
A0008941molecular_functionnitric oxide dioxygenase NAD(P)H activity
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
A0045454biological_processcell redox homeostasis
A0046210biological_processnitric oxide catabolic process
A0046872molecular_functionmetal ion binding
A0051410biological_processdetoxification of nitrogen compound
A0098869biological_processcellular oxidant detoxification
B0005344molecular_functionoxygen carrier activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008379molecular_functionthioredoxin peroxidase activity
B0008941molecular_functionnitric oxide dioxygenase NAD(P)H activity
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0034599biological_processcellular response to oxidative stress
B0045454biological_processcell redox homeostasis
B0046210biological_processnitric oxide catabolic process
B0046872molecular_functionmetal ion binding
B0051410biological_processdetoxification of nitrogen compound
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 3001
ChainResidue
AGLN79
AVAL80
AGLN82
BGLY83

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 5001
ChainResidue
BHOH5040
BHOH5044
BHOH5058
BGLY2
BARG6
BTYR16
BASP17
BHIS22

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 5002
ChainResidue
APRO108
ASER109
AHOH5030

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 5003
ChainResidue
AVAL34
AARG35
AHOH5051
BALA75

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CYN A 145
ChainResidue
APHE33
AHEM144

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CYN B 145
ChainResidue
BPHE33
BHEM144

site_idAC7
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 144
ChainResidue
APHE45
APHE46
ATHR49
AARG53
ALEU54
APHE61
APHE62
ATYR72
AGLY74
AALA75
AMET77
AVAL80
AHIS81
AILE86
APHE91
AVAL94
AILE119
ALEU122
AVAL126
ACYN145
AHOH5098

site_idAC8
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM B 144
ChainResidue
AHOH5018
BPHE45
BPHE46
BTHR49
BARG53
BLEU54
BLYS57
BPHE61
BPHE62
BTYR72
BGLY74
BALA75
BMET77
BVAL80
BHIS81
BARG84
BILE86
BPHE91
BVAL94
BILE119
BVAL126
BCYN145
BHOH5084

Functional Information from PROSITE/UniProt
site_idPS01213
Number of Residues21
DetailsGLOBIN_FAM_2 Protozoan/cyanobacterial globins signature. FFaaalGGPepYtGAp....MkqvH
ChainResidueDetails
APHE61-HIS81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: proximal binding residue
ChainResidueDetails
AHIS81
BHIS81

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon