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5C6E

Joint X-ray/neutron structure of equine cyanomet hemoglobin in R state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005833cellular_componenthemoglobin complex
A0015671biological_processoxygen transport
A0020037molecular_functionheme binding
A0031838cellular_componenthaptoglobin-hemoglobin complex
A0046872molecular_functionmetal ion binding
A0048821biological_processerythrocyte development
B0005344molecular_functionoxygen carrier activity
B0005833cellular_componenthemoglobin complex
B0015671biological_processoxygen transport
B0020037molecular_functionheme binding
B0031721molecular_functionhemoglobin alpha binding
B0031838cellular_componenthaptoglobin-hemoglobin complex
B0046872molecular_functionmetal ion binding
B0048821biological_processerythrocyte development
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue HEM A 201
ChainResidue
ATYR42
AASN97
ALEU101
ALEU136
ACYN202
ADOD302
ADOD319
ADOD331
APHE43
AHIS45
AHIS58
ALYS61
ALEU86
AHIS87
ALEU91
AVAL93

site_idAC2
Number of Residues4
Detailsbinding site for residue CYN A 202
ChainResidue
ALEU29
AHIS58
AVAL62
AHEM201

site_idAC3
Number of Residues10
Detailsbinding site for residue HEM B 201
ChainResidue
BPHE41
BPHE42
BHIS63
BSER70
BPHE71
BHIS92
BLEU96
BASN102
BLEU141
BCYN202

site_idAC4
Number of Residues3
Detailsbinding site for residue CYN B 202
ChainResidue
BHIS63
BVAL67
BHEM201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: distal binding residue => ECO:0000250|UniProtKB:P80044
ChainResidueDetails
BHIS63

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue => ECO:0000269|PubMed:561852, ECO:0007744|PDB:1G0B, ECO:0007744|PDB:1IBE, ECO:0007744|PDB:1IWH, ECO:0007744|PDB:1NS6, ECO:0007744|PDB:1NS9, ECO:0007744|PDB:1Y8H, ECO:0007744|PDB:1Y8I, ECO:0007744|PDB:1Y8K, ECO:0007744|PDB:2D5X, ECO:0007744|PDB:2DHB, ECO:0007744|PDB:2MHB, ECO:0007744|PDB:2ZLT, ECO:0007744|PDB:2ZLU, ECO:0007744|PDB:2ZLV, ECO:0007744|PDB:2ZLW, ECO:0007744|PDB:2ZLX
ChainResidueDetails
BHIS92

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylvaline => ECO:0000250|UniProtKB:P02086
ChainResidueDetails
BVAL1
ASER49

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
BSER44
ALYS11
ALYS40

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
BLYS59
BLYS82
BLYS144

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
BCYS93

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P69905
ChainResidueDetails
ATYR24

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ASER102
ASER124
ASER131
ASER138

site_idSWS_FT_FI9
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ATHR108
ATHR134
ATHR137

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PDB entries from 2025-06-18

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