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3NVU

Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion

Functional Information from GO Data
ChainGOidnamespacecontents
A0020037molecular_functionheme binding
B0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 200
ChainResidue
ALYS2
ALEU117
ATYR131
ASER133
AARG135
ALEU144
AILE145
ASER148
AHOH213
AHOH221
AHOH246
ALEU5
AHOH248
AOXY493
APHE78
ATYR85
APHE86
APHE94
AMET98
AHIS102
ALEU105

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OXY A 493
ChainResidue
ALEU5
APHE78
ATYR140
ALEU144
AHEM200

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 189
ChainResidue
AASN62
AGLU65
AHOH250

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 200
ChainResidue
BLYS2
BLEU5
BPHE78
BTYR85
BPHE94
BMET98
BHIS102
BLEU105
BTHR106
BALA115
BLEU117
BMET129
BTYR131
BSER133
BARG135
BLEU144
BHOH193
BHOH205
BHOH224
BOXY494

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OXY B 494
ChainResidue
BLEU5
BPHE78
BTYR140
BHEM200

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

222415

PDB entries from 2024-07-10

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