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2P0B

Crystal structure of chemically-reduced E.coli nrfB

Functional Information from GO Data
ChainGOidnamespacecontents
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEC A 201
ChainResidue
AALA23
AVAL71
AMET72
AARG73
AGLU76
AHEC202
AHOH213
AHOH379
ACYS24
ACYS27
AHIS28
AHIS57
APRO60
AHIS64
AARG65
AGLY67

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEC A 202
ChainResidue
ACYS24
AHIS28
AGLU33
AMET35
AHIS39
AVAL51
ATHR52
ACYS53
ACYS56
AHIS57
APHE74
ASER118
ALEU119
AHIS120
AHEC201
AHOH219
AHOH238

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEC A 203
ChainResidue
ALYS38
AHIS39
AVAL42
AILE43
AASN44
AASN55
APHE74
ACYS88
ACYS91
AHIS92
ACYS113
AHIS117
ALEU119
AASP124
AGLN127
AHEC204
AHOH214
AHOH215
AHOH348
AHOH375

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEC A 204
ChainResidue
ACYS88
AMET89
AHIS92
ALEU97
AALA100
APHE101
AHIS104
ACYS113
ACYS116
AHIS117
AHEC203
AHEC205
AHOH226
AHOH274
AHOH299
AHOH316

site_idAC5
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEC A 205
ChainResidue
AASN46
ATHR54
AASN55
AGLN59
ASER86
ASER90
APHE101
APRO103
AVAL106
AHIS107
ALYS110
AVAL111
ASER115
ACYS116
AARG134
AILE137
ACYS138
ACYS141
AHIS142
AGLN145
AHEC204
AHOH300
AHOH344
AHOH351
AHOH354

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: covalent => ECO:0000250
ChainResidueDetails
ACYS24
ACYS141
ACYS27
ACYS53
ACYS56
ACYS88
ACYS91
ACYS113
ACYS116
ACYS138

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: axial binding residue => ECO:0000250
ChainResidueDetails
AHIS28
AHIS57
AHIS92
AHIS117
AHIS142

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PDB entries from 2024-11-06

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