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3R0G

3D Structure of Ferric Methanosarcina Acetivorans Protoglobin I149F mutant in Aquomet form

Functional Information from GO Data
ChainGOidnamespacecontents
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 200
ChainResidue
ALEU70
AARG119
AHIS120
ALYS125
AASN126
ATYR141
APHE145
AILE146
ATRP185
AHOH197
AHOH205
ATYR73
AHOH209
AHOH219
AHOH243
APHE74
ATYR85
AVAL89
AARG92
APHE93
ATRP96
ATYR112

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A 3546
ChainResidue
AHOH218

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 3547
ChainResidue
ALYS191
AASP194
BHIS121
BARG122
BHOH222

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 3548
ChainResidue
ALEU27
AGLU30
BPRO68
BHIS69

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IPA A 4571
ChainResidue
APRO19
AASP24
BARG140

site_idAC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM B 200
ChainResidue
BLEU70
BTYR73
BPHE74
BTYR85
BVAL89
BARG92
BPHE93
BTRP96
BTYR112
BARG119
BHIS120
BASN126
BILE137
BTYR141
BPHE145
BILE146
BTRP185
BHOH198
BHOH212
BHOH216
BHOH240

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EPE B 3380
ChainResidue
AHIS121
AARG122
ATHR123
AGLY161
AHIS162
ATHR163
AHOH272
BLYS191
BTYR192
BASP194

221051

PDB entries from 2024-06-12

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