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3LAH

Structural insights into the molecular mechanism of H-NOX activation

Functional Information from GO Data
ChainGOidnamespacecontents
A0020037molecular_functionheme binding
B0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 200
ChainResidue
AMET1
ATHR113
APRO114
APRO115
ATYR131
ASER133
AARG135
AMET137
ALEU144
AHOH203
AIMD501
ALYS2
AIMD502
AILE5
APHE78
ATYR85
APHE94
AMET98
ALEU105
AALA112

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IMD A 501
ChainResidue
AILE5
APHE78
ATYR140
AHEM200

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IMD A 502
ChainResidue
AMET98
AGLY102
APRO114
APRO115
ALEU117
AHEM200

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM B 200
ChainResidue
BMET1
BLYS2
BILE5
BPHE78
BTYR85
BPHE94
BMET98
BLEU105
BALA112
BTHR113
BPRO115
BTYR131
BSER133
BARG135
BMET137
BTYR140
BLEU144
BILE145
BHOH193
BHOH209
BIMD501
BIMD502

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IMD B 501
ChainResidue
BILE5
BPHE78
BTYR140
BLEU144
BHEM200

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IMD B 502
ChainResidue
BMET98
BGLY102
BPRO115
BLEU117
BHEM200

Functional Information from PROSITE/UniProt
site_idPS00217
Number of Residues26
DetailsSUGAR_TRANSPORT_2 Sugar transport proteins signature 2. FlGLIeGSskffkeeIsvEevergeK
ChainResidueDetails
APHE141-LYS166

246704

PDB entries from 2025-12-24

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