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1HM6

X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0001786molecular_functionphosphatidylserine binding
A0001891cellular_componentphagocytic cup
A0002250biological_processadaptive immune response
A0002376biological_processimmune system process
A0002548biological_processmonocyte chemotaxis
A0002685biological_processregulation of leukocyte migration
A0004859molecular_functionphospholipase inhibitor activity
A0005509molecular_functioncalcium ion binding
A0005544molecular_functioncalcium-dependent phospholipid binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005769cellular_componentearly endosome
A0005886cellular_componentplasma membrane
A0005929cellular_componentcilium
A0006909biological_processphagocytosis
A0006954biological_processinflammatory response
A0007165biological_processsignal transduction
A0007187biological_processG protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
A0008360biological_processregulation of cell shape
A0012506cellular_componentvesicle membrane
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0016328cellular_componentlateral plasma membrane
A0019834molecular_functionphospholipase A2 inhibitor activity
A0030036biological_processactin cytoskeleton organization
A0030659cellular_componentcytoplasmic vesicle membrane
A0031410cellular_componentcytoplasmic vesicle
A0031514cellular_componentmotile cilium
A0031901cellular_componentearly endosome membrane
A0032652biological_processregulation of interleukin-1 production
A0032743biological_processpositive regulation of interleukin-2 production
A0042102biological_processpositive regulation of T cell proliferation
A0042119biological_processneutrophil activation
A0042995cellular_componentcell projection
A0045087biological_processinnate immune response
A0045627biological_processpositive regulation of T-helper 1 cell differentiation
A0045629biological_processnegative regulation of T-helper 2 cell differentiation
A0045920biological_processnegative regulation of exocytosis
A0046872molecular_functionmetal ion binding
A0046883biological_processregulation of hormone secretion
A0050727biological_processregulation of inflammatory response
A0070062cellular_componentextracellular exosome
A0071385biological_processcellular response to glucocorticoid stimulus
A0071621biological_processgranulocyte chemotaxis
A0090303biological_processpositive regulation of wound healing
B0001786molecular_functionphosphatidylserine binding
B0001891cellular_componentphagocytic cup
B0002250biological_processadaptive immune response
B0002376biological_processimmune system process
B0002548biological_processmonocyte chemotaxis
B0002685biological_processregulation of leukocyte migration
B0004859molecular_functionphospholipase inhibitor activity
B0005509molecular_functioncalcium ion binding
B0005544molecular_functioncalcium-dependent phospholipid binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005768cellular_componentendosome
B0005769cellular_componentearly endosome
B0005886cellular_componentplasma membrane
B0005929cellular_componentcilium
B0006909biological_processphagocytosis
B0006954biological_processinflammatory response
B0007165biological_processsignal transduction
B0007187biological_processG protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
B0008360biological_processregulation of cell shape
B0012506cellular_componentvesicle membrane
B0016020cellular_componentmembrane
B0016323cellular_componentbasolateral plasma membrane
B0016324cellular_componentapical plasma membrane
B0016328cellular_componentlateral plasma membrane
B0019834molecular_functionphospholipase A2 inhibitor activity
B0030036biological_processactin cytoskeleton organization
B0030659cellular_componentcytoplasmic vesicle membrane
B0031410cellular_componentcytoplasmic vesicle
B0031514cellular_componentmotile cilium
B0031901cellular_componentearly endosome membrane
B0032652biological_processregulation of interleukin-1 production
B0032743biological_processpositive regulation of interleukin-2 production
B0042102biological_processpositive regulation of T cell proliferation
B0042119biological_processneutrophil activation
B0042995cellular_componentcell projection
B0045087biological_processinnate immune response
B0045627biological_processpositive regulation of T-helper 1 cell differentiation
B0045629biological_processnegative regulation of T-helper 2 cell differentiation
B0045920biological_processnegative regulation of exocytosis
B0046872molecular_functionmetal ion binding
B0046883biological_processregulation of hormone secretion
B0050727biological_processregulation of inflammatory response
B0070062cellular_componentextracellular exosome
B0071385biological_processcellular response to glucocorticoid stimulus
B0071621biological_processgranulocyte chemotaxis
B0090303biological_processpositive regulation of wound healing
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 801
ChainResidue
AARG124
ALYS128
AHOH1010
AHOH1015
AHOH1063

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 802
ChainResidue
BARG234
BARG235
BGLN238
BHOH961

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 803
ChainResidue
ATHR145
AARG147
AHOH810
AHOH879

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 804
ChainResidue
AARG234
AARG235
AGLN238
AHOH887
AHOH1053

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 805
ChainResidue
AARG124
ALYS128
AGLY129
AHOH1012
AHOH1013
AHOH1082

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 806
ChainResidue
ALYS81
AGLN117
AHOH872
AHOH983
AHOH985

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 807
ChainResidue
AARG212
BARG213
BTHR216
BHOH900

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 808
ChainResidue
BARG124
BLYS128
BHOH1202

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 809
ChainResidue
BARG124
BLYS128
BGLY129

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 800
ChainResidue
BTHR145
BARG147
BHOH827

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 811
ChainResidue
AASN249
BTHR291
BHIS293
BLYS294
BHOH1136

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 812
ChainResidue
BGLY174
BASP175
BLYS257
BHOH848
BHOH990
BHOH1144

Functional Information from PROSITE/UniProt
site_idPS00223
Number of Residues53
DetailsANNEXIN_1 Annexin repeat signature. GVdeatiieiLtkRtnaQrqQikaaYlqekgkpLdeaLkkaltGhleevAlaL
ChainResidueDetails
AGLY59-LEU111
AGLY131-LEU183
AGLY215-VAL267
AGLY290-LEU342

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues52
DetailsBINDING: BINDING => ECO:0007744|PDB:1MCX
ChainResidueDetails
ATHR64
ALEU137
AGLU139
ATYR176
AGLY215
ALEU218
AVAL220
AGLY258
AILE260
AGLU261
AVAL266
AILE65
ATHR291
AHIS293
ATHR295
AGLY333
ATYR335
AGLU336
AALA341
BTHR64
BILE65
BGLU67
AGLU67
BGLY102
BGLU105
BALA110
BTHR132
BGLU134
BTHR136
BLEU137
BGLU139
BTYR176
BGLY215
AGLY102
BLEU218
BVAL220
BGLY258
BILE260
BGLU261
BVAL266
BTHR291
BHIS293
BTHR295
BGLY333
AGLU105
BTYR335
BGLU336
BALA341
AALA110
ATHR132
AGLU134
ATHR136

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by CTSG => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
AGLY31
BGLY31

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
APHE7
BPHE7

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by TRPM7 => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
AGLN10
BGLN10

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by EGFR => ECO:0000269|PubMed:3020049
ChainResidueDetails
ALYS26
BLYS26

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
ATYR39
APHE42
BTYR39
BPHE42

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
ASER46
ALEU141
BSER46
BLEU141

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10107
ChainResidueDetails
AALA63
BALA63

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
ASER244
ALYS317
BSER244
BLYS317

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) => ECO:0000250
ChainResidueDetails
ATHR24
BTHR24

site_idSWS_FT_FI11
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
ALYS337
BLYS337

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P04083
ChainResidueDetails
AASN219
BASN219

site_idSWS_FT_FI13
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000250|UniProtKB:P10107
ChainResidueDetails
AASN262
BASN262

237735

PDB entries from 2025-06-18

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